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Tag - Akitio
CES: Akitio launches two-bay Thunder3 Duo Pro Thunderbolt 3 enclosure
Device manufacturer Akitio today unveiled the Thunder3 Duo Pro, the industry's first hardware RAID and display dock solution designed for the new Thunderbolt 3 technology. The Thunder3 Duo Pro offers fast data transfers with the added flexibility of a DisplayPort video output in a small form factor.
Akitio brings 16TB SSD Thunderbolt 2 array to NAB
Akitio today announced the availability of the new 12TB Thunder2Quad Mini Thunderbolt 2 portable storage engineered with 4K workflows in mind. With up to 22 hours of 4K video storage on tap and, the Thunder2Quad is available as an enclosure only or populated with up to 12TB of storage in the form of four 2.5-inch 3TB SSDs.
Review: Akitio Thunderbolt Thunder Dock
Akitio has expanded its line of Thunderbolt accessories with its new Thunder dock. With eSATA, FireWire 800, USB 3.0 and Thunderbolt pass-through, the new accessory aims to provide a sensible set of additional ports for most MacBooks manufactured in the past three years. Check out our full review to see if the Thunder is a must-have desk accessory.
Review: Akitio MyCloud Mini Personal Cloud Server
Mobile devices are great, if a bit constrained on space sometimes. Those 8,000 pictures and five captured videos from the last concert attended tend to eat space if not offloaded. Akitio may have a solution -- the MyCloud Mini Personal Cloud Server. Leveraging a home Internet connection and associated network, the diminutive device -- when equipped with a 2.5-inch hard drive -- can store some data external to the device, allowing a mobile device to access stored files either remotely, or when inside the home network confines. Electronista took a look at the device, but is it worth your time?
Review: Akitio Neutrino U3+ USB 3.0 hard drive enclosure
As notebook computers continue to grow in popularity, 2.5-inch hard drives have become one of the most popular upgrades. Most of the drives that are pulled out of a computer end up collecting dust, but Akitio's Neutrino U3+ enclosure promises to give life back to unused drives, or serve as a basis for custom external storage. In our full review, we take a closer look at the USB 3.0-equipped enclosure.
Now AAPL Stock: 136.66 ( + 0.13 )
Cirrus creates Lightning-headphone dev kit
Apple supplier Cirrus Logic has introduced a MFi-compliant new development kit for companies interested in using Cirrus' chips to create Lightning-based headphones, which -- regardless of whether rumors about Apple dropping the analog headphone jack in its iPhone this fall -- can offer advantages to music-loving iOS device users. The kit mentions some of the advantages of an all-digital headset or headphone connector, including higher-bitrate support, a more customizable experience, and support for power and data transfer into headphone hardware. Several companies already make Lightning headphones, and Apple has supported the concept since June 2014. http://bit.ly/29giiZj
Apple Store app offers Procreate Pocket
The Apple Store app for iPhone, which periodically rewards users with free app gifts, is now offering the iPhone "Pocket" version of drawing app Procreate for those who have the free Apple Store app until July 28. Users who have redeemed the offer by navigating to the "Stores" tab of the app and swiping past the "iPhone Upgrade Program" banner to the "Procreate" banner have noted that only the limited Pocket (iPhone) version of the app is available free, even if the Apple Store app is installed and the offer redeemed on an iPad. The Pocket version currently sells for $3 on the iOS App Store. [32.4MB]
Porsche adds CarPlay to 2017 Panamera
Porsche has added a fifth model of vehicle to its CarPlay-supported lineup, announcing that the 2017 Panamera -- which will arrive in the US in January -- will include Apple's infotainment technology, and be seen on a giant 12.3-inch touchscreen as part of an all-new Porsche Communication Management system. The luxury sedan starts at $99,900 for the 4S model, and scales up to the Panamera Turbo, which sells for $146,900. Other vehicles that currently support CarPlay include the 2016 911 and the 2017 models of Macan, 718 Boxster, and 718 Cayman. The company did not mention support for Google's corresponding Android Auto in its announcement. http://bit.ly/295ZQ94
Apple employees testing wheelchair features
New features included in the forthcoming watchOS 3 are being tested by Apple retail store employees, including a new activity-tracking feature that has been designed with wheelchair users in mind. The move is slightly unusual in that, while retail employees have previously been used to test pre-release versions of OS X and iOS, this marks the first time they've been included in the otherwise developer-only watchOS betas. The company is said to have gone to great lengths to modify the activity tracker for wheelchair users, including changing the "time to stand" notification to "time to roll" and including two wheelchair-centric workout apps. http://bit.ly/2955JDa
SanDisk reveals two 256GB microSDXC cards
SanDisk has introduced two 256GB microSDXC cards. Arriving in August for $150, the Ultra microSDXC UHS-I Premium Edition card offers transfer speeds of up to 95MB/s for reading data. The Extreme microSDXC UHS-I card can read at a fast 100MB/s and write at up to 90MB/s, and will be shipping sometime in the fourth quarter for $200. http://bit.ly/294Q1If
Apple's third-quarter results due July 26
Apple has advised it will be issuing its third-quarter results on July 26, with a conference call to answer investor and analyst queries about the earnings set to take place later that day. The stream of the call will go live at 2pm PT (5pm ET) via Apple's investor site, with the results themselves expected to be released roughly 30 minutes before the call commences. Apple's guidance for the quarter put revenue at between $41 billion and $43 billion. http://apple.co/1oi1Pbm
Twitter stickers slowly roll out to users
Twitter has introduced "stickers," allowing users to add extra graphical elements to their photos before uploading them to the micro-blogging service. A library of hundreds of accessories, props, and emoji will be available to use as stickers, which can be resized, rotated, and placed anywhere on the photograph. Images with stickers will also become searchable with viewers able to select a sticker to see how others use the same graphic in their own posts. Twitter advises stickers will be rolling out to users over the next few weeks, and will work on both the mobile apps and through the browser. http://bit.ly/29bbwUE


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Biostimulants Market is anticipated to reach USD 2.91 billion by 2021. For broad acre crops, biostimulants prove to be beneficial since they improve productivity in adverse conditions like high heat, salinity, draught or floods. Raw material for biostimulants are available and row crops like cereals and oilseeds are also making use of such stimulants. Therefore, the biostimulants market growth is majorly driven.
Browse detailed TOC, Tables, Figures, Charts and Companies mentioned in Biostimulants Market @ http://www.absolutereports.com/10198108
This report provides thorough information on the following aspects of Biostimulants Market:
Biostimulants market size:
Seaweed extracts and microbial amendments segment market size is expected to grow at the fastest rate. Reasons behind this growth is that seaweed extracts are better at improving structure of soil, aeration in the soil, seed germination and production. They also increase tolerance for biotic and abiotic stress.
Market Drivers of Biostimulants Industry:
Market Restraints of Biostimulants Industry:
Market Opportunities in Biostimulants Industry:
Market Challenges in Biostimulants Industry:
Companies profiled in this report are:
On the basis of Region, the Biostimulants Market:
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Biostimulants market overview:
Factors influencing the market growth are explained in the reports. Biostimulants increase yield as well as quality, which is a major driving factor along with other factors like they require less investments. However, lack of awareness regarding their use may restrain the growth of the market. Developing countries demand for cost effective products that can increase yield. This demand offers promising opportunities for the market.
Biostimulants industry key players:
A detailed analysis of the competition is given in the report. This includes, activities like new product launch, mergers & acquisitions, agreements, etc. Company profiles of major players and study of their product, strategies and development are also given.
All the information in this report was collected through secondary research and verified through interviews with industry experts and decision maker.
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subset: commoncrawl


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Re: Nimes Sports Bar Tuesday 22 April 2008
Walk into any bar that looks hip, or any Irish/English pub and ask them, there are a few there, and I do remember one (an excellent one!) close the Arenes, can't remember its name or location though.
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Panda Express Gift Card $100
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Panda Express Gift Card $100 Our Mission is to deliver exceptional Asian dining experiences by building an organization where people are inspired to better their lives.
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There he was. Dark, brown locks, smoky grey eyes, and that 5 o'clock shadow that wason his face. He lifted his head, staring a her, and gave a small smile.She started to walk toward his table, slowly, as if waiting for him to change his mind. After all thatthey had been through, why now? Why now did he want to make things right. After the world thought he was dead, aftershe though he was dead. Aftershe wept and wept for months. Aftershe burned all of his things to keep his memory from haunting her. Why now?
She pulled out a seat and sat, liftingher sunglasses to the top ofher head.She took offher olive trenchcoat and took a deep breath. He positioned himself in a comfortable pose, he thought theymight be there for a while."Hello Kade," he began the conversation in his deep, british accent. Kade looked at the table, not daring to make eye contact.
"Darling, talk to me," he sweetly said, his hand about to caress her hair. But deep anger, depression, and hatred could neverlet him get thatclose again. With tears streaming from her eyes, Kade slapped him right on the face.
"That's for puttingme through years of suffering Roran," with that, Kade got up and left, heading down the corner of Main and South Boulevard. Roran sat there with a hand on his face, going over what had just happened.
"Wait!" Roran stood from his chair and ran towards Kade. When he got to the corner, Roran couldn't spot Kade in any direction. Hewinged it, pacing down South Boulevard. "Kade!" he called, echoeing through the buildings as he went on by. There she was! Roran quickly caught up up with her. "Gosh, peaches, you've made me chase you all over the city! What's wrong?" Roran exclaimed out of breath.
"You are!" Kade answered in a shrieky voice, "You've hurt me to my deepest, I've almost killed myself, the pain of losing you was too much!" Roran grabbed around her body, taking her closer to his. Kade struggled and struggled, but his grasp was way too tight on her body. Roran wouldn't let go, he lovedher too much for words, so much in fact that he couldn't help but lay a kiss on her lips. Kade thought that was the last thing to expect on a day like this.
"So?" Roran asked, wondering if she enjoyed the kiss as much as he did. Kade held silent for a moment. She looked deep in thought. Were there sparks or had the magic fade? As she picked at her brain, she only felt one feeling towards Roran, that one feeling and nothing else.
"Roran" Kade began, "Our life together was perfect, a complete fairy tale before the incident. I never thought I'd be happier with any other man but yo-"
"Kade!" a stranger called from the end of the street corner. The two looked at him, two cups of coffee in his hands and a big, bright smile on his face. "Who's that?" Roran asked with a curious look.
"See," Kade started, "it's just not that I don'tlove you anymore, it's that..... well I....you see...I've found someone else."
"Oh," Roran replied with a streak of realization through him.
"I'm sorry Ror," with one last stare, Kade left Roran, left him for her new love. A new Kade has entered the world. A more confident, hopeful, and stronger one. One that Roran would never have anything to do with, never again. When Kade got to him, he handed her the cup of coffee, a vanilla mocha frappachino, her favorite, the one Roran had bought her so many times. They both turnedthe corner with a smiling face, and Kade, ready to forget him forever.
© Copyright 2017 Breettey Skye. All rights reserved.
Status: Finished
Genre: Romance
Oh my gosh, you have so much talent! I absolutely loved it! You hooked me in right from the start. I must admit I was a bit confused at first, but you're right; it began to make more sense. But I feel as if there's something else, some other part to the story that you were holding back. Maybe more background, maybe continue the ending, I don't know what it was that seemed to be missing, but I think that you should very well make this into a novel! And btw, I am absolutely looking forward to writing a short story with you! You have such talent.
I know it's a good a idea to add that something to it, but that's not the way I write. I write with the sense of imagination. I like people to think of the ending for themselves. I like to hear what people think how it ends. It makes writing a little more intersting. But, of course, I don't write like that all the time, it's just mainly for my short stories. You should read A Friend, A Brother, And A True Love. That's one of my favorites.
very good
i love your writing style
it leaves people wanting more
you're a really good writer with true talent. i must say i'm jealous. i can write, but not the way you do. this story is perfect. i love it. but i don't understand why you think it leaves off the ending. i think it's complete the way it is. if you added any more, it would seem redundant. this kind of ending is much prefered to one that seems too explanatory and not conclusion-like. anyways, good work. keep it up. :]
Book / Action and Adventure
Short Story / Romance
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BMW 5 series four door saloon (1988 to 1996)
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Carbox HS BMW 5 E34 (88 to 96) JV10-2016
- This high-sided liner fits behind the rear seats.
- A Carbox high-sided liner will help to keep your car boot in immaculate condition, and protect its resale value.
All our prices include VAT at 20%


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What happened to liberal Democrats, and their concerns about civil liberties and government surveillance of American citizens?
Liberals once hated the CIA. And they loved the Russians. Yeah, you can look it up.
And their liberal friends in liberal Hollywood made movie after movie about the dangers of The Deep State and its awesome surveillance powers. One of the best was "Three Days of the Condor," with liberal icon Robert Redford fighting the malevolent CIA boss John Houseman, who longed for "the clarity" of world war.
Years later, Edward Snowden became the liberal demigod and Wikileaks was their winged chariot of truth and beauty. Liberals fretted...


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The cult skincare brand has teamed up with the "godfather of street style blogs" Scott Schuman aka The Sartorialist for a Father's Day-friendly campaign.
Much has been written about Schuman, but it is a little-known fact that he took his first steps as a street style photographer taking pictures of his daughters at a playground in New York.
For Kiehl's, he went back to that very same playground, shooting fathers with their kids for an "awww"-inducing photo series that is similar to a campaign released by competing brand Dove last year.
But thanks to hipster authority Schuman, Kiehl's can take it one step further, also launching a limited-edition men's grooming bag, filled with the blogger's favorite products of the brand, including Facial Fuel face wash and moisturizer, lip balm, shaving cream, and a scrub soap.
The bag is available for $55.50 at selected Kiehl's stores and online.
Watch a behind-the-scenes video of the campaign shoot at http://youtu.be/du26lUGhlEg.Reuse content


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Rachel Eliza Griffiths
MULE & PEAR (New Issues Poetry & Prose) --- These poems speak to us with voices borrowed from the pages of Alice Walker, Jean Toomer, Toni Morrison, Valerie Martin, Edward P. Jones, Nella Larsen, and others - voices that still have more to say. Each struggles beneath a yoke of dreaming, loving, and suffering. These characters converse not just with the reader but also with each other, talking amongst themselves, offering up their secrets and hard-won words of wisdom, an everlasting conversation through which these poems voice a shared human experience. Now available for pre-order on Amazon (Pub date: September 5, 2011).
2011 Rachel Eliza Griffiths. All Rights Reserved.


text: 000 FGUS75 KRIW 231650 ESFRIW WYC003-250450- Hydrologic Outlook National Weather Service Riverton WY 950 AM MST THU FEB 23 2017 ...Colder temperatures through early next week will decrease flooding due to ice jams along the Big Horn River... High temperatures along the Big Horn River are expected to be into the upper 20s to lower 30s from Friday through Tuesday of next week. Low temperatures along the the Big Horn River are expected to be between 8 to 20 degrees from Friday through Tuesday of next week. Flooding from ice jamming expected to decrease through early next week with the expected colder temperatures. Also, no significant new ice is expected to form on the the Big Horn River with forecasted low temperatures next week. People who live next to the Big Horn River should still be vigilant of the possibility of flooding due to ice jams. Ice jams are very unpredictable and can occur very quickly with little or no notice. Move to higher ground if flooding is occurring due to ice jams. Graphical forecasts are available at: http://water.weather.gov/ahps2/index.php?wfo=riw Visit weather.gov/riverton and select the rivers & lakes tab for graphical forecasts and additional information. $$ jtfahey


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If you can read this, please take a step back. Mens T-Shirt
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Wedding Cheesecakes
Looking for recipes for wedding cheesecakes? Taste of Home has the best wedding cheesecake recipes from real cooks like you, featuring reviews, ratings, how-to videos and tips.
Recipe Spotlight
One slice is never enough of this dreamy cheesecake. The rich filling and golden glaze tempt your taste buds with a delicate hint of lemon.—Taste of Home Test Kitchen, Greendale, WisconsinGet Recipe
More Wedding Cheesecakes


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A man who's still a virgin, has a very very rare disease that only allows him to have sex 7 times in his life. After he's used up all 7 of the chances, he'll never be able to have an erection and ejaculate, which means he will lose his ability to have sex for the rest of his life. So far, he has wasted 2 times while masturbating, so he's left with only 5 more chance to have sex. He has to save those precious bullets, but at the same time he desperately want to lose his virginity.
Source: MU
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Sakuranbo Syndrome
Ore x Yome
Kono S o, Mi yo!
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Seyfucoidan uses cultured mozuku from Tonga, 100%, is produced.
■Fucoidan is an essential ingredient for the seaweed.
It is a slimy ingredients and fucoidan mozuku seaweed, kelp and seaweed to cover the surface. In 1913, by scholars in Sweden are secreted from the mucous membrane tube of seaweed that has been identified. Thought there is working to protect the seaweed in the fierce tidal flow, is the essential ingredient for seaweed. In recent years, health power of fucoidan together attention, nutritional supplementation, and the beauty has piled up various studies around the world.
■Because the low-molecular absorption is different.
It was yesterday because some sugars are intertwined in complex, known as polymer polysaccharide fucoidan poorly absorbed in the body.
[Seyfucoidan] Was succeeded by up to 500 low-molecular-molecular weight of mosque Kiss itself in the manufacturing process, greatly enhance the absorption from the stomach and intestines.
* Food is stomach and digestion and absorption in the small intestine that most big molecular weight is 3000-4000.
It is seyfucoidan is one-sixth of great absorption power.
As healthy as drinking, quantity limits, but sometimes one 30 ml and 60 ml drink on an empty stomach.
For more information, please contact by phone or email.
|Seyfucoidan (sugar-free) 900 ml 2pcs
|The name
|Soft drinks
|Name of raw material
|Seaweed extract (mozuku low molecular extract), vitamin C, acidulant (citric acid), vitamin B6, NICOTINAMIDE, vitamin B1, vitamin B2
|Content amount
|1800 ml (900ml×2 book set)
|How to save
|Avoid direct sunlight, please store in a cool and dry place.
Save in the refrigerator after opening.
|Sales person
|Co., Ltd. evseysey Horiuchi
|Suggested usage
|Quantity, but as a general health during one 30 ml and 60 ml drink on an empty stomach.
Standard of drinking water are enclosed products * for more information, visit.
|Manufacturers suggested retail price
|(Tax included)
|Ads responsibility
|Good luck in medicine
|Co., Ltd. evseysey Horiuchi
|Country of manufacture
This product cannot be shipped to United States from the store.
Please contact the store for further information.


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Syncing a libferris filesystem with an XML file or database
With libferris, FUSE, and rsync, you can synchronize a filesystem with a dissimilar data source.
Admins use rsync to snchronize two filesystem trees. With a few tricks, you can use FUSE and libferris with rsync to synchronize a filesystem with another data source such as an XML file or a PostgreSQL database. Libferris is a user address space Virtual FileSystem (VFS) that lets you mount almost any data source as a filesystem. Examples of data sources libferris can mount include XML files, Berkeley db4 files, rpm packages, relational databases, LDAP servers, web servers, and applications like XWindow, Emacs, xmms, Amarok, and Firefox. Libferris also includes evolving support for mounting web services. For example, you can interface a libferris directory with a photo-sharing website like 23hq or Flickr. In this article, I will discuss some of the possibilities for using rsync to synchronize a libferris filesystem with an XML file or database.
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Munich Plans to Ditch Linux and Go Back to Windows
A major setback for the Linux desktop.
Linux Kernel 4.10 Comes with New Security Features
Improved support for GPU in virtualization.
OpenSUSE Site Hacked
News site for the openSUSE community falls victim to a Wordpress exploit.
LibreOffice Goes Online with 5.3 Release
The source code is available online.
Microsoft Brings Clear Linux OS to Azure
One out of three virtual machines on Microsoft Azure Cloud run Linux.
ASUS Announces a Single-Board Computer
The form factor of the board makes it a drop-in replacement for Raspberry Pi.
Red Hat Releases RHEL 6.9 Beta
Makes it easier for customers to move workloads into container-centric applications.
SUSE Working on a New Operating System Called MicroOS
SUSE's answer to container-centric operating systems.
Biggest Kernel Release Ever
Linux 4.9 is the biggest release in terms of number of commits.
CentOS Linux 7 (1611) Released
The latest version of the official RHEL clone is here.


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The Peerless-AV Modular Mounts Line features a full range of products that can fulfill multiple requirements from a limited number of SKUs. With the universality of the components, configure your own perfect custom flat-panel display or projector mounting solution for any application.
The Modular Mount Line was developed with the professional AV installer in mind. Designed around a 2" (50mm) diameter pole, the line is ideal for new projects as well as for upgrading existing installations.
The MOD-FPSKIT100-B Ceiling Mount Kit comes with all of the components required to ceiling mount a single 32-60" flat panel display. As a part of the Peerless-AV™ Modular Series, it can be expanded with additional Modular accessories (sold separately) to accommodate additional displays, configurations to achieve the perfect custom mounting solution.
Single Display Up to 3' (1m) Height


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Based on early bioinformatic studies on a handful of species, the frequency of structural disorder of proteins is generally thought to be much higher in eukaryotes than in prokaryotes. To refine this view, we present here a comparative prediction study and analysis of 194 fully described eukaryotic proteomes and 87 reference prokaryotes for structural disorder. We found that structural disorder does distinguish eukaryotes from prokaryotes, but its frequency spans a very wide range in the two superkingdoms that largely overlap. The number of disordered binding regions and different Pfam domain types also contribute to distinguish eukaryotes from prokaryotes. Unexpectedly, the highest levels – and highest variability – of predicted disorder is found in protists, i.e. single-celled eukaryotes, often surpassing more complex eukaryote organisms, plants and animals. This trend contrasts with that of the number of domain types, which increases rather monotonously toward more complex organisms. The level of structural disorder appears to be strongly correlated with lifestyle, because some obligate intracellular parasites and endosymbionts have the lowest levels, whereas host-changing parasites have the highest level of predicted disorder. We conclude that protists have been the evolutionary hot-bed of experimentation with structural disorder, in a period when structural disorder was actively invented and the major functional classes of disordered proteins established.
Citation: Pancsa R, Tompa P (2012) Structural Disorder in Eukaryotes. PLoS ONE 7(4): e34687. doi:10.1371/journal.pone.0034687
Editor: Laszlo Buday, Hungarian Academy of Sciences, Hungary
Received: December 13, 2011; Accepted: March 8, 2012; Published: April 5, 2012
Copyright: © 2012 Pancsa and Tompa. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Funding: This work was supported by the The Research Foundation-Flanders Odysseus grant G.0029.12. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
Competing interests: The authors have declared that no competing interests exist.
Deciphering protein structures has been instrumental in understanding the molecular principles of life. Yet, the recent most exciting development in structural biology is the recognition that many proteins (intrinsically disordered proteins, IDPs) or regions of proteins (intrinsically disordered regions, IDRs) exist and function without a well-defined structure [1], [2], [3]. The existence and functioning of IDPs/IDRs demand a radical extension of the structure-function paradigm to encompass their non-conventional functional modes. The functional advantages of structural disorder are manifested either directly, in functions termed entropic chains, or in molecular recognition, in the form of adaptable binding [4], uncoupling specificity from binding strength [5] or increasing the speed of interactions [6], [7], among others. Due to these advantages, an elevated level of structural disorder can be found in proteins involved in signaling and regulation, and structural disorder is often associated with disease, such as cancer and neurodegeneration [7].
The functional advantages and functional types of IDPs/IDRs predisposes them for roles in complex organisms, in broad agreement with the observed phylogenetic distribution of structural disorder [8], [9], [10]. Based on previous studies on a few genomes available at the time (usually comparing predicted disorder in 4–5 eukaryotes to bacteria and archea), it has become generally accepted that structural disorder is significantly higher in eukarytoes than in prokaryotes, expressed by the notion that structural disorder correlates with complexity. Besides these comparative studies, the level of disorder was only addressed in particular phylogenetic groups, such as bacteria [11], [12], archaea [13] or a few protists within eukaryotes [14], [15]. More recent studies presented large-scale analyses, without trying to derive general conclusions [16]. The suggested correlation with complexity was directly addressed for organisms of known complexity measures (number of different cell types) [17]. It was found that disorder has a tendency to increase in evolution, but its correlation with complexity within eukaryotes is marginal.
Therefore, even these limited studies have raised certain caveats to the above generalizations, and suggested exceptions to the seemingly simple and general rule. For example, studies on the distribution of predicted structural disorder in prokaryotes has shown wide variations as a function of growth temperature, with mesophiles an thermophyles covering a very broad range from ∼1.5% to ∼25% but hyperthermophiles having much less [11], [12]. Archaea were also found to show wide disorder distribution, with strong genomic variations depending on habitat and lifestyle [13]. Turning to eukaryotes, Apicomplexan protists - single-celled eukaryotes - have shown unexpectedly high levels of predicted disorder, way exceeding that of apparently more complex metazoan organisms [14]. Similar conclusions were drawn in a study of a handful of early-branching protists [15], which again showed a high level of predicted disorder surpassing the average of eukaryotic proteins in SwissProt. It was raised that structural disorder may be associated with the parasitic lifestyle of these organisms.
As apparent from this short overview, structural disorder has not been systematically and comparatively analyzed in eukaryotes. Apparently, one of the reasons is a very fast advance in sequencing efforts, due to which about two-thirds of known eukaryotic genomes became available in the past five years or so. Furthermore, the results of distinct studies are hard to compare, because they rely on different disorder predictors usually based on different principles and having significantly different rates of confidence [18], [19], [20]. In addition, often related but different measures of structural disorder (frequency of disordered residues, frequency of proteins with a long IDR, or frequency of mostly disordered proteins) are applied, which again impedes comparisons and sound generalizations. Therefore, we decided to predict and compare structural disorder in 194 available eukaryotic proteomes (and 87 reference prokaryotes) with the IUPred algorithm [21], [22]. We extended and complemented these calculations with predictions of the prevalence of Pfam domains and comparing disorder within and outside domains, because: i) disordered regions often harbor binding motifs for domains [23], ii) disordered regions often function by acting as linkers between flanking domains, and iii) structural disorder may also be present in Pfam domains themselves [24]. The novel data on the phylogenetic distribution of structural disorder, Pfam domain types, and their varied correlation in different types of species refine previous limited generalizations and provide novel insight into the evolutionary and functional implications of structural disorder.
Eukaryotic, prokaryotic and archaeal proteomes
Most of the eukaryotic proteomes were downloaded from the complete proteome set of the UniProt database [25], and some additional ones from the RefSeq database [26]. To avoid redundancy, we usually used only one proteome for species for which multiple strains are available (such as, in the case of S. cerevisiae, for example). In the case of non-pathogenic higher-order organisms, we only used one representative proteome for several very closely related species within one genus (such as in case of the Drosophila genus); for pathogens, we kept the proteomes of all species. For all the species analyzed, we indicate the source and date of actual downloading in Supplementary Table S1.
For a comparison, proteomes of all the reference Bacteria (69) and Archaea (18) were also downloaded from the UniProt database (cf. Supplementary Table S2 and S3, respectively). In case of the eukaryotic proteomes, the downloaded sequence data also contained all the known isoforms. To avoid redundancy, all the proteomes were filtered for 90% sequence identity with the CD-HIT V4.5.4 program [27]. For every filtered proteome, the number of proteins and the average protein length was calculated. Proteomes thus filtered were used for further analysis.
Prediction of structural disorder and disordered binding sites
Structural disorder and disordered binding sites were predicted by the ANCHOR algorithm [16] which incorporates the IUPred algorithm for disorder prediction [21], [22]. From predicted IUPred disorder scores, we calculated distinct measures of disorder. First, the average disorder score for all proteins was calculated by averaging the value of disorder scores for individual residues across the entire protein. The ratio of disordered residues was calculated as the percentage of residues within the protein with a disorder score ≥0.5. This value was also calculated for regions identified as Pfam domains (for prediction of Pfam domains, see next section) and also for regions outside Pfam domains. Here we divided all the proteins of the proteomes in which at least one Pfam family, domain or repeat was predicted into two parts, one containing all the predicted Pfam domains, the other containing the rest of the protein. For these we calculated the ratio of disordered residues separately. The values calculated for the regions outside the domains were grouped together with the values for those proteins in which no Pfam domains were found. From all the values determined, measures for entire proteomes were calculated as follows. The average disorder of proteins was averaged for the whole proteome, yielding the value referred to as average disorder in the proteome. The ratio of disordered residues (disorder score ≥0.5) was also averaged for all proteins, termed thereafter as the average ratio of disordered residues in proteins. The ratio of proteins with at least one long (≥30 consecutive residues with a score ≥0.5) disordered region and the ratio of amino acids within these regions was also calculated. From the results of binding-site predictions by ANCHOR, only those sites were kept, which are marked as "real" by ANCHOR. The overall number of disordered binding sites and the average number of disordered binding sites per protein was calculated for every proteome. All calculated data are found in Supplementary Table S1, S2, and S3 for Eukaryotes, Bacteria and Archaea, respectively.
Prediction of Pfam domains
With the PfamScan method [28], all Pfam-A families, domains and repeats were predicted for every protein in our datasets. Pfam-B domains were neglected because of much lower quality of the underlying HMM profiles. The total number of different types of domains/families/repeats was calculated for every proteome. In the text we refer to these regions as Pfam domains, irrespective of their actual type (i.e. family, domain or repeat). All the calculated data are found in Supplementary Table S1, S2, and S3 for Eukaryotes, Bacteria and Archaea, respectively. The ratios of disordered residues as defined in the previous section were also calculated and averaged for the Pfam domains and also regions outside domains.
Phylogenetic groups
There are various existing phylogenies for eukaryotes, we implemented our data with the one used by UniProt except for the Opisthoconta kingdom, which contains Fungi and Metazoa as well as some other protists. Because of the large amount of species in these two groups, we decided to handle them separately from the remaining two species in Opisthoconta, so in the figures only the two species are marked to be Opisthoconta and the others in this kingdom are separated to Fungi and Metazoa groups.
Structural disorder, domains and motifs in the three superkingdoms of life
Based on much more species than in previous analyses, we first asked if the distribution of predicted disorder in Bacteria, Archaea and Eukaryota reflects those obtained in prior studies [8], [9], [10]. Here we collected 194 eukaryotes, 69 bacteria and 18 archaea (for a complete list, cf. Supplementary Table S1, S2 and S3) and predicted structural disorder in all proteins in all proteomes by the IUPred algorithm [21], [22]. From the disorder score, two primary measures of disorder were calculated: the average disorder score values for all proteins averaged for all the proteomes through the entire superkingdom (Figure 1A) and the ratios of disordered residues within the proteins (with a score ≥0.5), also averaged for the proteomes of the entire superkingdom (Figure 1B). (Other measures of structural disorder, such as the ratio of proteins with at least one long (≥30 consecutive disordered residues) disordered region and the ratio of amino acids within these regions, were also calculated (cf. Supplementary Table S1, S2 and S3), but are not plotted because they showed very similar qualitative trends).
Structural disorder was predicted by the IUPred algorithm [21], [52] for all the proteins in the proteomes collected; the average disorder (A) and the ratio of disordered residues (B) were calculated for the three superkingdoms, Bacteria, Archaea and Eukaryote. Disordered binding sites (C) were predicted by the ANCHOR method [16] and averaged for all proteins in all proteomes in the three superkingdoms. The search for Pfam domains (D) was carried out by the PfamScan algorithm [28]. The number of different Pfam domains was calculated in all proteomes and averaged in the three superkingdoms. On every panel, the horizontal line in the box shows the median of the data, the mean is indicated by a small square, and the upper and lower edge of the box indicates the 75 and 25% of the data, respectively. The upper and lower error bars show the 90 and 10% of the data respectively, the upper and lower cross represents 99% and 1% of the data, while the maximum and minimum value within the dataset is indicated by short horizontal lines.
Overall, predicted structural disorder shows the trends established earlier, eukaryotes having higher averages than both prokaryotic groups, Bacteria being clearly higher than Archaea [8], [9], [10]. Due to the large number of proteomes, it is now clear that there is no straightforward correlation between disorder and phylogeny, because both prokaryotes and eukaryotes show large variations with extensive overlaps, with all the reference prokaryotes being higher than the lowest of eukaryotes, for example. Therefore, we asked further what possibly distinguishes prokaryotes from eukaryotes, thus we also predicted and compared their number of disordered binding regions by the ANCHOR method [16] (Figure 1C) and the number of different Pfam domain types occurring in their proteomes (Figure 1D). As a first conclusion, all three features seem to distinguish between prokaryotes and eukaryotes to some extent, and their combination might be a strong descriptor of protein phylogeny (a similar conclusion was also reached in [17]).
Structural disorder in all eukaryotes
Next, we asked about the reason of this lack of clear separation between the large phylogenetic groups. Previous studies of bacterial proteomes have shown large inter-species variations possibly linked with lifestyle and habitat [11], [12], [13]. Here we calculated the ratio of disordered residues for all the 194 eukaryotic proteomes (and also other measures, cf. Supplementary Table S1, showing the same trends). The values plotted as a function of the number of proteins in the proteome (Figure 2) are scattered over a broad range (0.016 to 0.368), and show a general but not strictly monotonous increase with proteome size. Mostly single-celled organisms are responsible for the deviation from linearity, because they cover the entire range, reaching both above and below multicellular organisms (plants and animals). Multicellular organisms consistently have intermediate values, most of them falling between 0.15 and 0.25. In addition, the level of structural disorder in protists is not random but distinct clades show characteristic differences, very much in line with their pathogenic status and lifestyle. Free living and host-changing organisms have the highest levels, whereas endosymbionts and obligate intracellular pathogens completing their life cycle in the same host have the lowest levels of structural disorder (cf. also Discussion).
On the main plot the average ratio of disordered residues (with an IUPred score ≥0.5) in proteins of all eukaryotic proteomes is shown as a function of the number of proteins in the given proteome. Large phylogenetic groups are indicated with different colors, as defined on a small plate. In the insert, the average and standard deviation for the different groups is given, by applying the same color code as in the main plot.
Number of Pfam domain families in proteomes
Structural disorder shows very large inter-species variations among eukaryotes, which might also be reflected in – or be a reflection of – the number of types of protein domains in the different species. This expectation is based on IDPs/IDRs often carrying out their function in association with folded domains, either as linkers in multidomain proteins [29], [30] or as motifs/disordered domains [23], [24] binding in and induced folding process to cognate domains [5]. To this end, we asked how the number of distinct Pfam domains (domain types) changes with the number of proteins in proteomes and if it reflects the evolutionary division between prokaryotes and eukaryotes. We predicted the number of distinct Pfam-A families, domains and repeats for every protein in our datasets with the PfamScan search algorithm [28]; summary data for the entire superkingdoms are already shown in Figure 1D.
Unlike structural disorder, the number of domain types shows a monotonous increase with proteome size throughout the superkingdom of eukaryotes, from as low as 200 domains to as high as 4500. The similarities and differences carry important evolutionary and functional information, as addressed below.
The correlation of structural disorder, domains and short binding motifs
As seen, both structural disorder and the number of Pfam domains in the proteome increase in evolution, roughly in proportion to the number of proteins in the proteomes (Figure 2 and Figure 3, respectively), with apparent and significant differences, though. As suggested in the Introduction, disordered proteins/regions function either as entropic chains (linkers between domains) or via molecular recognition, in which they use either short binding motifs [23] or disordered domains [24]. In this sense, the evolution of domains and disordered regions is intertwined and is often inseparable. To visualize this interdependence, and possible critical differences, we plotted the average ratio of disordered residues as a function of the number of different Pfam domains (Figure 4). The straight line fitted proves a good correlation between the two, however, certain groups show systematic deviations (see also Discussion). Fungi consistently tend to have more disorder than the average, whereas Metazoa have less (interestingly, among all the metazoans, the mosquito, Anopheles darlingi has the highest ratio of disordered residues in its proteins. This species of mosquito is the most important malaria vector in South America and it is capable of transmitting both Plasmodium falciparum and Plasmodium vivax. Whether its high disorder is related to this fact, remains to be seen).
Pfam domains were predicted for all eukaryotic proteomes with PfamScan [28]. On the main plot the number of different types of Pfam domains is shown as a function of the number of proteins in the given proteome. Large phylogenetic groups are indicated with different colors, as defined on a small plate. In the insert, the average and standard deviation for the different groups are given, by applying the same color code as in the main plot.
The average ratio of disordered residues (with a score ≥0.5) in proteins of the eukaryotic proteomes, is shown as a function of the number of different Pfam domains found. Large phylogenetic groups are color coded, as defined on a small plate. The linear fit of the data is shown as a dashed line. Certain species are named and certain groups are encircled and marked, as explained and discussed in the text.
Pathogenic protists, such as Trypanosoma and Leishmania species (Euglenozoa) or Plasmodium species (Alveolata) have much more disorder than expected. Viridiplantae are clearly separated into two groups by the line: multicellular land plants tend to have less disorder, whereas single-celled algae have more disorder than expected. Obligate intracellular parasites, such as Microsporidia (Fungi) and the endosymbiotic nucleomorphs (Cryptophyta and Rhizaria), have very little of both in proportion: reduction of their genomes seems to have shaved all superfluous domains and disordered regions down to the acceptable minimum. Their detailed studies might help understand the types of proteins and functions that cannot exist without structural disorder.
The parallel increase of the number of domain types and the ratio of disordered residues may be conceived either as a result of an increase of disorder both within and outside domains and also as an increase only in the regions outside domains. Whereas disorder occurs with a notable frequency also within domains [24], we found that regions outside domains are about three times more disordered. To address the correlation of domains and disorder, we have directly calculated the level of disorder within and outside domains (Supplementary Figure S2). The two values show a very strong correlation (Figure 5), i.e. large evolutionary variations of disorder in eukaryotes results from parallel changes in disorder within and outside Pfam domains. There seem to be very little compensatory effects (e.g. low level of disorder in domains compensated by very high levels of disorder outside domains). There are a few significant exceptions, though. Pathogenic protists and Anopheles darlingi show significantly higher disorder outside their domains than expected, whereas obligate intracellular parasites Microsporodia and Nucleomorphs have much less. Apparently, these latter organisms have given up on all regulatory functions linked with disorder outside their domains. This feature is also apparent in the almost complete lack of disordered binding regions in them (see next section).
The average ratio of disordered residues (with a score ≥0.5) in proteins of the eukaryotic proteomes, within regions outside Pfam domains is shown as a function the same value within Pfam domains. Large phylogenetic groups are color coded, as defined on a small plate. The linear function showing a parallel increase of disorder within and outside Pfam domains in most species is marked by a dashed line. Certain groups of species show significant deviation from this linear dependence, as explained and discussed in the text.
Turning to recognition motifs directly, it should be noted that these are short (typically 3–15 residues in length [31]), they contain very little sequence information and their prediction from sequence is fraught with extremely high false positive rates. An unbiased prediction of disordered binding sites relies on assessing their interaction energy with a potential partner. We used this algorithm, ANCHOR [16], to predict the number of disordered binding sites in all proteins in all the proteomes (Supplementary Table S1, S2 and S3, already plotted for the superkingdoms, cf. Figure 1C) and plot it as a function of the number of domains (Figure 6). Again, there is an overall correlation between these two measures, which shows and exponential character, with more domains being associated with disproportionately more binding sites. This also somewhat explains the deviations from the linear regression on Figure 4. Fungi and pathogenic Trypanosoma, Leishmania (Euglenozoa) and Plasmodium (Alveolata), which all have more disorder then expected based on the number of their Pfam domains (Figure 4), are clearly distinguished here. Pathogenic organisms use a lot of this "excess" disorder for short binding motifs (cf. also Figure 5), probably involved in pathogen-host interactions, as already suggested for viruses [32]. Fungi, on the other hand, may have more of their disordered regions probably serving as linkers (entropic chains) in large multidomain proteins.
The overall number of predicted disordered binding sites in eukaryotic proteomes predicted by the ANCHOR algorithm [16] is shown as function of the number of different Pfam domains. Large phylogenetic groups are color coded, as defined on a small plate. Certain species and certain groups are marked and/or named, as explained and discussed in the text. The increasing (exponential) function marked by the dashed line is no fit by any model, it is only drawn to guide the eye. Homo sapiens has a larger apparent proteome size, because it has been analyzed at greater depth and the number of identified isoforms exceeds that of other mammals even after sequence identity filtering.
In this paper the first full analysis of structural disorder in all eukaryotic proteomes sequenced thus far is presented. Several general conclusions can be drawn, some corroborate and/or extend previous notions derived from much more limited data, others provide completely new insight into the evolution, distribution and likely functional importance of structural disorder. Our starting point is that this study reaffirms previous assertions that the number of proteins in proteome is not a good measure of complexity [17], confirmed here by the whole body of data (cf. for example the comparable size of the proteome of humans and the ciliated protist Paramecium tetraurelia, or plants of very similar complexity that have undergone genome duplications).
Therefore, we concentrated our study on structural disorder, the number of different Pfam domain types and disordered binding motifs in all the eukaryotic proteomes available today. The classical notion of the field is that structural disorder has contributed to the evolutionary transition from prokaryotes to eukaryotes [8], [9], [10]. By comparing 194 eukaryotic genomes to 69 (bacterial)+18 (archaeal) reference prokaryote genomes, we do find that this view is largely correct, but only with serious reservations. Prokaryotes do have a lower average disorder than eukaryotes (e.g. mean disorder score, bacteria: 0.211, archaea: 0.185, eukaryotes: 0.30), but both large groups extend over a very broad range of predicted disorder values (prokaryotes: 0.12 to 0.35, eukaryotes: 0.1 to 0.41). The view that eukaryotes contain more disorder than prokaryotes is an oversimplification, meaning that structural disorder does not simply depend on the complexity of the organism and does not define the phylogenetic group to which the organism belongs [17]. Rather, it represents a rapidly evolving modality which contributes to the fast appearance of novel functions, as already suggested for all prokaryotes [11] and archaea [13]. A decreased level of disorder seems to reflect adaptation to extreme conditions [11], or a nutrient-rich, stress-free (lenient [33]) intracellular environment, whereas an elevated level indicates that the organism leads a varied lifestyle in which it can change between habitats, most apparent in the case of host-changing pathogens. A comparison of superkingdoms suggests that the number of disordered binding sites per protein and the number of different Pfam domains is also significantly different between prokaryotes and eukaryotes. Their range of values (average number of disordered binding sites, prokaryotes: 0.072 to 2.93, eukaryotes: 0.11 to 9.4; Pfam domain types, prokaryotes: 376 to 2417, eukaryotes: 196 to 4400) separate large superkingdoms better, showing significantly less overlap.
The comparison of the different measures provide further insight: the number of domain types shows a rather monotonous increase in evolution, whereas the level of disorder shows an overall increase but large evolutionary fluctuations in certain clades, first of all in protists. This difference probably reflects that the creation of novel domain types is very demanding and is an event of low probability: multiple mutations within a sufficiently long region have to accumulate for a stable and functional fold to arise [34]. In accord, the complement of domain types available within a phylogenetic group does not fluctuate on a short timescale. Disorder seems to follow an entirely different path. IDPs evolve fast, accepting many more point mutations, insertions and deletions than globular proteins [35]; even repeat expansions are often observed in IDPs [36]. Its length-distribution follows a power-law (in humans, but probably also in other species), with many short regions but also a significant incidence of very long disordered regions [37]. In contrast with domains, which have been created steadily during evolution [38], structural disorder has the capacity of rapid appearance and disappearance, much contributing to evolutionary innovation, even on relatively short time-scales [39]. Intriguingly, the strict proportionality of disorder within and outside domains shows that disorder does have the potential to invade domains, probably increasing their functional diversity even within one family.
Further complicating their seeming independence is that structural disorder and domains cannot exist and function without each other. For example, multidomain proteins cannot exist without disordered linkers, as seen in the case of scaffold proteins [29]. Structural disorder is also often involved in molecular recognition, when a short disordered motif [31], [32] or even domain [24] undergoes induced folding in the presence of a partner, which is almost invariably a folded domain [5]. Due to this, the two basic types of function of disordered proteins (entropic chains and binding motifs) seem to diverge in this sense, because the number of motifs (that require domains as binding partners) follows pretty closely the expansion of domain families, probably because their reasonable number and varieties is limited by the number of cognate domains they can bind to. This is not the case of motifs that pathogens use to interact with their host [32] and also not for IDPs that function as entropic chains, which have functions either independent of domains [40] or their length is not limited by the domains connected [29], [30], [37].
Therefore, the simple evolutionary trends result in distinct taxon-specific combinations of the number and actual types of domains and the ratio of disorder, as apparent from many observations in our study. Large and complex organisms, such as metazoans and plants have a high and rather even level of disorder. Fungi are more disordered than Metazoa or the Viridiplantae, and they also show more variation. Microsporidian intracellular parasites showing extreme small genome size and very low amount of structural disorder and certain plant pathogens which have very high amount of structural disorder, like the maize pathogen Sporisorium reilianum. Among single-celled eukaryotes (protists), on the other hand, we also find the less disordered organisms (Cryptophyta, which are endosymbionts) and the most disordered ones (one Alveolata – Toxoplasma gondii –, and some fungi). It is apparent that obligate parasites and symbionts (the most extreme being endosymbiotic plastids, nucleomorphs) have delegated many of their genes/functions to the host, and have undergone a tremendous genome reduction, this we have also seen in the thermal adaptation of bacteria [11]. On the other hand, free-living organisms, which have to change habitat and have to respond to varying environmental challenges, always have a very high level of disorder. This is also the case with host-changing parasites, rapid evolutionary adaptation of which occurs by creating structural disorder, as already witnessed in the case of apicomplexan parasites [14] and some early-branching pathogenic and non-pathogenic protists [15]. This probably explains why the species show a very high amount of disorder in the Trypanosoma genus, these have a complex life cycle and host-changing pathogenic life style. The Alveolata Cryptosporidium muris, which does not require a vector and is capable of completing its life cycle within a single host, has low ratio of disorder in its proteome (cf. Figure 4). On the other hand, the absolute recorder is the apicomplexan parasite Toxoplasma gondii, because more than 65% of its proteins have at least one long (≥30 consecutive residues) disordered region (Supplementary Table S1). Probably the complex life cycle and the broad range of mammalian hosts represent such a variable environment for this parasite that demands its high amount of disorder and fast rate of evolution. Among the unicellular organisms the Alveolata kingdom shows the highest deviation in disorder content. Many of them have a very high average protein size as well (Supplementary Figure S1), so it seems that their proteins abound in long disordered regions.
The case of pathogens can be rationalized (as also suggested for viruses [32], [41], [42]) by four, somewhat opposing, challenges these organisms face: i) they have to evade the immune system of the host, ii) they have to effectively interact with the host for invasion and iii) also for deregulating host metabolism for their own purposes, and iv) they have to do it with as compact a genome as possible. In these, the advantages of structural disorder are clearly apparent in the pathogenic protists [15]. In addition, the large variation of structural disorder in protists can also be viewed as an evolutionary relic of the role structural disorder played in the rise of eukaryotic organisms, because several novel disorder-related protein functional groups appeared early in eukaryotes, such as transcription factors [43], signaling proteins [29], transmembrane receptors [44], cytoskeletal proteins [45], [46], [47], proteins involved in membrane trafficking [48] and chromatin organization [49], [50], [51]. Further, hub proteins involved in multiple protein-protein interactions, thought to be critical in organizing interactomes of complex organisms, also have been noted for their elevated disorder [52], [53], [54].
In conclusion, we have selected and analyzed structural disorder in 194 genomes, far more than it was possible in previous comparative studies [8], [9], [10]. Our studies reaffirm that structural disorder distinguishes eukaryotes from prokaryotes, but its frequency in both large groups spans a very wide and overlapping range, and prokaryotes can only be clearly separated from eukaryotes if the number of disordered binding regions and different Pfam domain types are also taken into consideration. Extremes of predicted disorder are found in protists, where it correlates strongly with lifestyle. Low levels are observed in obligate intracellular parasites and symbionts, whereas high levels are observed in host-changing parasites. Our interpretation of these and many other particular observations is that protists have been – and still are – the evolutionary hot-bed of experimentation with structural disorder, resulting in rapid adaptive changes in response to environmental challenges.
Supporting Information
Figure S1.
Structural disorder and protein length in Eukaryotes. The average ratio of disordered residues (with a score ≥0.5) in proteins of the eukaryotic proteomes, is shown as a function of the average length of proteins in the given proteome. Large phylogenetic groups are color coded, as defined on a small plate. The oval indicates that most species fall within a central range. Certain pathogenic and endosymbiotic species named fall outside, either because they have very long proteins or lower than average disorder.
Figure S2.
Structural disorder within and outside Pfam domains. The average ratio of disordered residues (with a score ≥0.5) in proteins of the eukaryotic proteomes is calculated separately for regions identified as Pfam domains (A) and regions outside Pfam domains (B). Large phylogenetic groups are color coded, as defined on a small plate. The linear function showing a parallel increase of disorder within and outside Pfam domains in most species is shown as a dashed line.
Table S1.
Calculated data for Eukaryota. All the calculated data mentioned in methods for every eukaryotic taxon is included.
Table S2.
Calculated data for Bacteria. All the calculated data mentioned in methods for every bacterial taxon is included.
Author Contributions
Conceived and designed the experiments: RP PT. Performed the experiments: RP PT. Analyzed the data: RP. Wrote the paper: RP PT.
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text:
[Date Index] [Thread Index] [Author Index]
Re: How do I force Log[Exp[x]]=x
ComplexExpand[Log[E^x]] does the trick. Kevin -- Kevin J. McCann Johns Hopkins University APL Bart Killam <sasrbk at unx.sas.com> wrote in message news:87tp95$5ia at smc.vnet.net... > > For real x, Log[Exp[x]]=x. For general complex x > Mathematical leaves this expression unevaluated. I > have tried Log[Exp[x/;Im[x]=0]], but this give a result > of 0. > > How do I tell Mathematica that I want the expression > simplied for real x ? Thanks for any help.


text:
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Like what preceded it in the form of 'Millennial Projections' (1982), this collection of short prose is also comprised of sixteen stories, and again it is an intensely philosophical and ideological... More > project that is, however, more self-consciously avant-garde and determined to allow subjectivity, whether in first-person narrative or thought processes, its share of the narrative limelight. This is especially so of the title piece, 'A Selfish Man' (who is, of course, self-ish in the best sense of the word) but it's also characteristic, on a completely different structural basis, of the last piece, 'Twelve Thinkers', who have more in common with one another than might at first seem to be the case, despite their different occupations! The cover features a self-photo of John O'Loughlin in somewhat 'Steppenwolfian' mode taken in Salthill, Galway, in 2010.< Less
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Bugs are Beautiful
Posted in the Bugs Forum
1 - 20 of 31 Comments Last updated Feb 13, 2012
#1 Aug 22, 2008
Ribbet, ribbet, ribbet,ribbet, Ribbet.
ribbet, ribbet,ribbet, Ribbet,ribbet, ribbet,ribbet, Ribbet...Ribbet, ribbet, ribbet,ribbet, Ribbet.
ribbet, ribbet, ribbet, Ribbet...Ribbet, ribbet.
Ah, the sweet symphony of Bug Thugs! Welcome to the garden! Here, you will find a wide variety of fruits and vegetables on which to dine. Under the spreading Chestnut tree that shades you from a hot summer day, some of the finest lady bugs are preparing a feast. How glad I am to welcome you aboard. There will be an offsite event later this evening followed by tea and refreshments for all Lady Bugs! Hope to see you here, and look forward to your thoughts and comments!
Bugs are Beautiful
#2 Aug 22, 2008
OK. I just put the coffee on and the beer is chilling. Champagne is on ice. There is Crème brûlée, a fresh fruit tart, chocolate pudding cake and vanilla bean ice cream for the down homers, and rum cake with a glazed icing as well.
I hope the cushions on the lounge chairs are comfy, and I have turned on the jaccuzi. Anybody need a suit, or will there be skinny dipping by moonlight?
#3 Aug 22, 2008
Skinny dipping?...I can't believe you would even make such a suggestion!
Have you been drinking?
#4 Aug 22, 2008
What's a matter their Alien.. It is right up your alley.. lol
#5 Aug 22, 2008
Why, yes, I have. Why do you ask? LOL I've also been trying to "fix" my computer. It talks when I don't want it to, and it tells me I've won something I don't care about winning. Aughhh!!!
There are so many mysteries in life. For example, we had our seventeen year cicada invasion this summer. Those bugs sure can squeal!!! They'll sing to you loud enough you can't have a conversation outdoors.
What's new with you, Alien? Been playing any games with any beetles lately?
#6 Aug 22, 2008
Champagne and jaccuzi goes hand in hand..
Were all adults here... Birthday suits works just fine with me... We are respectable Patriots..
#7 Aug 22, 2008
I am resisting the temptation to be the bug that bites. LOL I've been visiting the Hinterlands, but I'm back for a snack! Lovely to see you, Gecko! Are you green? And, do you eat ladybugs? OMG! Don't answer that question. What was I thinking?
#8 Aug 22, 2008
Eats ladybugs? Yes, I do believe he does. He's freaky like that.
#9 Aug 22, 2008
Oh Gecko, you have NO idea what's up my alley!
Did you bring me something to drink?
#10 Aug 22, 2008
Well, as long as he's like that, we may have to muzzle him as soon as he has a beer and some dessert. Otherwise, there could be trouble, because this is a family site, and I don't mean THAT kind of family. LOL
I've got to go fling a mop around some floors, but I check back a little later to find out how much progress has been made in clearing the land of any and all vegetation. Thank GAWD there are no exterminators anywhere in the vicinity. I just hate those guys in the green jumpsuits. They remind me of prisoners in county lockup being brought before the judge and appearing live on your local news. Yeah. They were probably exterminators before they got caught murdering innocent bugs. That's ok. When they get zapped in the electric chair, we come in and take over and pick the bones. LOL I told you I'd been drinking again.
#11 Aug 22, 2008
You are so spoiled.. Tequilla with fresh sliced lemon and salt as usual..
So what's up your Alley?
Have anything to do with green stuff being on your face? lol
Interesting how you jumped on the name, "Alien." LOL
#12 Aug 22, 2008
Of course I am green...
Do I eat ladybugs? LMAO I am shocked at you Bugs..
I have a good idea what you were thinking.. lol
Them after thouights can be something else...
#13 Aug 22, 2008
Ladybugs are good...
No more freaky than the name you chose...
Which is very fitting I might add.. lol
#14 Aug 22, 2008
I don't eat Ladybugs, Bugs.. I just lick them...
To keep the dust off of their backs.. lol
I know you run a clean outfit here...
Alien will have it corrupted in no time though.. lol
#15 Aug 22, 2008
See you over at the bar. I'm gonna' float like a butterfly and sting like a bee! I'm just a ladybug looking at the end of summer and nothing to lose. ;-)
#16 Aug 23, 2008
Did someone say BEER! BBBBEEEEELLLLCCCCHHHHH! Sorry had a few on the way over <Big Grin>.
The food sound great BB but if you don't mind I am kind of a pretzels and steak bug only because it compliments the beer so well. LOL!
Skinny dipping huh? Sounds like you like to live on the wild side there BB? By chance are any of the bugs that are skinny dipping GREEN? Here about some of the strange things those green bugs do! Scary really! <Shutter>
#17 Aug 23, 2008
"Are you green? And, do you eat ladybugs?"
Just how much have you had to drink to ask that question there BB?
#18 Aug 23, 2008
Hehehehehe! I have exterminators for dinner! Such easy pickins'!
#19 Aug 23, 2008
Well Gecko if you saw the first Men in Black movie you would understand the name Alien in regards to bugs. Sad ending though the bugs lost! I swear humans I just don't get them.... LOL!
#20 Aug 23, 2008
Sounds to me like Gecko's brain is in the gutter! I am so glad I covered my virgin ears! Oh my eating Ladybugs! LOL!
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This summer, Public Services was delighted to have Lucia Ibarra, one of the Library's Eastside High School interns, work with us. Lucia's project was to rehouse a previously unprocessed collection of World War II letters and note any interesting observations or information along the way. The incredibly detailed notes she took will be used to create a finding guide (to be completed by December), but we wanted to share her description of her summer experience working with this archival collection:
I am pleased to announce that the Muñoz Family's Atari Collection (M2010) is processed and open for research. The collection is 11 linear feet and consists of an Atari 800XL home computer, color monitor and complete set of peripherals. The collection also includes 127 consumer software titles published between 1980 and 1987.
The Muñoz Family's Atari Collection is representative of early home computing in the 1980s when software and hardware manufacturers created products for nontechnical users wishing to use computing for entertainment (i.e. gaming) and practical uses in the home (i.e. personal finances and education). This collection compliments the Stephen M. Cabrinety Collection in the History of Microcomputing, ca. 1975-1995 (M0997) which contains software, computer hardware, peripheral devices, hand-held games, and computer industry literature documenting the microcomputing gaming industry during its formative years.
The Muñoz family generously gave their collection to Stanford University, Special Collections in 2012 and the collection was processed thanks to the efforts and talent of Melissa Pincus who worked for Public Services this summer. Melissa created the collection's finding guide which can be accessed through the collection's catalog record:
Social Justice at Stanford, an exhibit showing in the Bender Room of Green Library beginning September 30, explores the theme of social justice as revealed through a selection of materials from the Stanford University Archives documenting 20th century civil rights and social protest movements.
Walking around campus, one can readily see the impact of Stanford's Arts Initiative. Joining the existing Cantor Arts Center are several new buildings, including the Bing Concert Hall, which opened in 2013, the Anderson Collection at Stanford University, which opened on September 21st, and the growing structure that will be the McMurtry Building, slated to open in 2015.
In parallel with this new focus on the arts, the MSS division in Special Collections has worked over the last year with Peter Blank and Anna Fishaut at the Art & Architecture Library, in identifying and funding the preservation and processing of four recently acquired art collections. Some of the projects will include selected reformatting of audio-visual elements, processing of digital files, additional digitization efforts, and collaboration with the libraries' Department of Conservation and the Art Library's Visual Resources Center.
The Manuscripts Division is thrilled to announce that the Benoit Mandelbrot Papers are now open for research. A finding aid to the collection is available on the Online Archive of California and materials are pageable through the catalog record in Searchworks.
The papers document the life and work of Benoit Mandelbrot, maverick mathematician and pioneer of fractal geometry. The collection contains biographical material, personal and professional correspondence, drafts and typescripts for books and articles, subject files, and reprints. The collection also contains a significant amount of research data, including notes, plots, graphs, and computer-generated visualizations of fractals. Also included are teaching materials, administrative records, awards, and materials related to publicity events, such as posters and flyers announcing conferences and lectures focusing on fractals or related topics. Other formats present in the collection include photographs, audiovisual material, and computer media, as well as an extensive amount of fractal and fractal-related artwork.
The Archives is pleased to announce that it has acquired the papers of two noted scholars of women's studies: Marilyn Boxer and Karen Offen.
Marilyn Boxer (Ph.D, UC Riverside) is emeritus professor of history at San Francisco State University and former lecturer and scholar at the Institute for Research on Women and Gender at Stanford. She has held administrative appointments at San Diego State University, including Chair of the Department of Women's Studies (1974-1980) and Dean of College of Arts and Letters (1985-1989); as well as at San Francisco State University where she served as Vice-president for Academic Affairs (1989-1996). Boxer is the author of When women ask the questions: creating women's studies in America (1998). She has also co-edited three books: Socialist women: European socialist feminism in the nineteenth and early twentieth centuries (1978); Connecting spheres: European women in a globalizing world, 1500 to the present (1987); and Clara Zetkin: National and International Contexts (2012). In 2004, Boxer received the Helen Hawkins Feminist Activist Award for Betterment of Women's Lives.
In 1985, Steve Jobs gave Meneuz complete access to NeXT and he spent the next decade photographing over seventy companies, innovators, and investors in Silicon Valley. The Computer History Museum has a current exhibit up in their lobby of Meneuz's photographs that runs through September 7th - Fearless Genius: The Digital Revolution in Silicon Valley 1985–2000. The images in this exhibit are part of over 250,000 negatives in the Douglas Meneuz photography archive located in Stanford University Libraries' Dept. of Special Collections. Over 8,000 images are currently delivered online through SUL's Image Gallery.
We are happy to announce that Lucy Waldrop will join Special Collections in September as the project archivist on the Helen and Newton Harrison papers project. This is an NEH-funded project and will conclude in February 2016. Lucy comes to us from Wichita State University, where as a project archivist, she processed several large collections including that of photographer and film director Gordon Parks. The Harrison collection is a significant acquisition and this preservation and processing project is one of several art projects being undertaken by Special Collections in collaboration with the Art Library in the coming year.


text:
I continue to grub goldenrod out of the "swamp" (drier areas thereof)
- is probably 50% weeded. Not trying to get rid of all of it, but it
has monoculture aspirations! Receipt of Jason's ashes now has me
shifting attention to the shade garden to prepare his final resting
place. Cleaned up the perennial beds, removing some excess oriental
poppies in favor of asters. Need to do some plant shifting - the
amsonia I planted grew a lot bigger than I realized. Found a
bottlebrush buckeye seedling hiding with the oenothera next to the
house - definitely needs a new location. And then, there is the
drudgery of hose dragging... I knew there was a drought when even the
shrubs in the shad garden were wilting! We got .3 inch of rain over
the weekend. Not nearly enough, but had to rejoice anyway.
Cathy, west central IL, z5b
On Jul 4, 2005, at 6:01 PM, Donna wrote:
> Hope everyone had time to spend with friends, enjoy the holiday,
> eat bbq,
> and all the other holiday wishes.
> I had three days off in a row!
> Managed to make a huge dent in working in the yard along with
> socializing at
> night. Man am I tired!
> Both beds that have been cleaned out- ok, some started the weed
> thing again,
> but got the soil turned amended, planted, mulched and watered...DH
> decided
> to expand the one bed thru the fence and made this much larger than I
> imagined at 4AM while I was sleeping... Looks a tad spars, but will
> fill out
> and in the long run turn out better.
> They promised a cool weekend- yah right, maybe for Pam, but I was
> dieing out
> there, blasting myself with the hose to keep cool!
> Today they promised bad thunderstorms... yeah right- not a drop!
> Rich, just
> a tad south please...missed them by maybe 10-15 miles north of me.
> I feel
> sorry for those effected, although we need the rain, some were very
> damaging, power out, trees down, you know the routine.
> Anyways, a couple more weekends and I will be done with the
> remodeling of
> the yard... sort of, DH still hasn't worked on that darn train layout!
> So what did everyone else do?
> Donna
> ---------------------------------------------------------------------
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text:
Magento Ecommerce Website
This project received 150 bids from talented freelancers with an average bid price of $3804 USD.Get free quotes for a project like this
Project Budget$3000 - $5000 USD
Total Bids150
Project Description
Hi There,
We're seeking a professing magneto developer / team to create our ecommerce website. Our extensive knowledge about graphic design will force us to only accept the best most reliable experience applicant.
We believe that our project needs the perfect brain in order to bring it alive. We will be expecting a lot of customization to fit our project specifications.
Only high skilled magneto developers are needed. A sample of previous projects should be presented along with client contact references and few samples of your ability levels.
Skills Required
Looking to make some money?
- Set your budget and the timeframe
- Outline your proposal
- Get paid for your work
Hire Freelancers who also bid on this project
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- Forbes
- The New York Times
- Time
- Wall Street Journal
- Times Online


text:
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Organisational Capability and Competitive Advantage
Edited by Charles Harvey Geoffrey Jones
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Organisational Capability and Competitive Advantage by Charles Harvey
Book DescriptionFirst Published in 1992. Routledge is an imprint of Taylor & Francis, an informa company.
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Book DetailsISBN: 9780714634579
(216mm x 140mm x 15mm)
Pages: 216
Imprint: Frank Cass Publishers
Publisher: Taylor & Francis Ltd
Publish Date: 1-Jun-1992
Country of Publication: United Kingdom
Other Editions...
Books By Author Charles Harvey
Business History, Paperback (June 2014)
First Published in 1989. Routledge is an imprint of Taylor & Francis, an informa company.
Organisational Capability and Competitive Advantage, Paperback (June 2014)
First Published in 1992. Routledge is an imprint of Taylor & Francis, an informa company.
Breakout Strategy, Hardback (October 2006)
Introduces the 'fast track' concept, describing successful strategies that result in rapid business growth for any organization. This title features initiatives such as: create a value-based vision, give customers a value proposition, align what you do with customer desires, and balance 'hard' and 'soft' business to deliver on promises.
Business Elites and Corporate Governance in France and the UK, Hardback (December 2005)» View all books by Charles Harvey
Examines corporate governance from a comparative standpoint and looks beneath the surface at the exercise of power and authority in two distinct national business systems. This book aims to shed light on the mechanisms that govern the stability and regeneration of business elites against the backdrop of an increasingly global economy.
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