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Protein Folding and Neurological Disease

We often think of proteins are nutrients found in the food we eat and the main component of muscles, however, proteins are microscopic molecules located inside of cells which actually perform a variety of fundamental roles. The function of a protein depends on its shape, and when protein formation goes awry, the resulting misshapen proteins can cause numerous health issues, such as when proteins neglect their essential roles or when they form a sticky, clumpy clutter inside of cells. Protein formation is an error-prone procedure and mistakes along the way have been associated with neurological diseases.  


There are approximately 20,000 to over 100,000 unique types of proteins found inside a common human cell. Why so many? Proteins are the workhorses of the human cell. By way of instance, several of these proteins are structural, lending stiffness and rigidity to thin neurons or muscle tissues. Other proteins shuttle them to new places and bind to specific molecules and others catalyze responses. A property of proteins is possible through diversity and specificity in their role when they fold.  


Why Proteins Fold into a Functional Shape


A protein generally begins in the cell as a lengthy chain of about 300 building blocks known as amino acids. There are 22 different types of amino acids and their order decides what protein chain will fold onto itself. After folding, two types of structures will generally form. Several regions of the protein chain coil into slinky-like formations known as “alpha-helices,” while other regions fold into zigzag patterns known as “beta-sheets,” which resemble the folds of a paper fan.  


Both of these structures may interact to form complex structures. In one protein structure, many beta-sheets wrap themselves around to form a hollow tube. The tube is also generally short where the overall structure resembles snakes (alpha-helices) emerging out of a can (beta-sheet tubing ). Moreover, several other protein structures with descriptive names include the “beta-barrel,” that the”beta-propeller,” the”alpha/beta-horseshoe,” as well as the “jelly-roll fold”.  


These intricate structures allow proteins to perform their variety of roles in the cell. The “snakes in a can” protein, when embedded into a cell membrane, creates a tube which enables traffic in and out of cells. Other proteins form contours with pockets known as “active sites” which are perfectly shaped to bind to a certain molecule like a lock and key. By bending into different shapes, proteins can do different functions. To draw an analogy, all vehicles are made from steel, while a bus, dump truck, crane, or Zamboni are shaped to execute their very own tasks however races are won by the slick shape of a racecar.  


Why Protein Folding Sometimes Fails


Protein folding ultimately allows a protein to take a functional shape, however, it’s an intricate procedure which can sometimes fail. According to research studies, protein folding can go wrong due to three major reasons:  


  1. A person may have a mutation which affects an amino acid in the protein chain, making it difficult for a specific protein to locate its favored fold or “native” state. This is how it is for mutations, such as those contributing to cystic fibrosis or sickle cell anemia. These mutations are found in the DNA sequence or “gene” which encodes one special protein. Therefore, these types of inherited mutations affect only that protein and its related function.
  2. On the other hand, protein folding failure can be seen as an ongoing and much more general procedure which affects several proteins. When proteins are made, the structure which reads the instructions from DNA to produce the long chains of amino acids can make errors. Researchers estimate that the ribosome makes mistakes in as many as 1 in every 7 proteins. These mistakes can make the proteins which are resultantly inclined to continue to fold improperly.
  3. Even though an amino acid chain does not have any mutations or mistakes, it may still not reach its own preferred folded shape because proteins don’t fold properly 100 percent of their time. Protein folding becomes much more difficult if the conditions in the cell change due to external factors such as temperature and acidity.


A collapse in protein folding can cause a variety of neurological diseases and researchers hypothesize that many health issues are associated with folding problems. There are two problems which exist in cells which don’t protein fold correctly.  


One type of problem, known as “loss of function,” results when not enough of a particular protein folds correctly, causing a lack of “specialized functions” necessary to perform a particularly important role. By way of instance, imagine a correctly folded protein is shaped to bind a toxin and split it into noxious compounds. Without enough of that protein accessible, the toxin will build-up to damaging levels. In another instance, a protein may be responsible for metabolizing sugar which can then be utilized by the cell for energy. The cell will grow due to lack of energy if not enough of this protein is accessible. The reason the cell becomes ill, in these cases, is because of a lack of one particular folded, functional protein. Cystic fibrosis, Tay-Sachs disease, Marfan syndrome, and some types of cancer are examples of health issues which result when one type of protein is unable to perform its role. Who knew that one type of protein out of thousands may be so significant?  


Proteins folding may also impact the overall health and wellness of the cell regardless of the utilization of the protein. When proteins fail to fold into their functional state, the consequent misfolded proteins could be contorted into shapes which are harmful to the crowded cell environment. Most proteins have sticky, “water-hating” amino acids which they bury deep inside their own core. Misfolded proteins utilize these parts on their exterior, such as a chocolate-covered candy which has been crushed to reveal a gooey center. These misfolded proteins commonly stick together to form clumps known as “aggregates.” Researchers discovered that the accumulation of misfolded proteins plays a fundamental role in several neurological diseases, including Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and Lou Gehrig’s (ALS) disease, however, researchers are still working to discover exactly how these misfolded molecules affect the well-being of the cells.  


One misfolded protein ultimately stands out from among the rest and it deserves particular attention. The “prion” protein in Creutzfeldt-Jakob disease, also known as mad cow disease, is an illustration of a misfolded protein gone rogue. This protein isn’t simply irreversibly misfolded, however, it also transforms other functional proteins into a similar twisted condition.  


How Cells Protect from Misfolded Proteins


Recent research studies have demonstrated that protein misfolding often occurs inside of cells. Fortunately, cells also have many systems in place and are accustomed to coping with this issue by refolding or destroying aberrant protein formations.   Appropriately known as chaperones, these structures accompany proteins throughout the folding procedure, enhancing a protein’s odds of folding properly and even allowing several misfolded proteins the opportunity to refold. Chaperones are proteins themselves. There are many distinct types of chaperones. A few chaperones supply safety to proteins, isolated from other molecules. Production of many chaperones is fostered when a cell encounters high temperatures or other states which can ultimately make protein folding more difficult, therefore, providing these chaperones the alias, “heat shock proteins.”  


The following line of cell defense against misfolded proteins is known as the proteasome. If misfolded proteins linger in the cell, they will be targeted for destruction by this structure, which chews proteins up and spits them out. The proteasome is similar to a center, permitting the cell to reuse amino acids to create proteins. The proteasome itself is not a single protein but many acting collectively. Proteins frequently interact to form larger structures. By way of instance, a human sperm’s tail is a structure made of various types of proteins which work together to produce a rotary engine which propels the sperm.  


Protein Folding and Misfolding Overview


Why is it that some misfolded proteins can evade systems such as chaperones and the proteasome? How can the neurological diseases previously mentioned above be caused by sticky misfolded proteins? Do some proteins misfold more often than others? These questions are at the forefront of research studies seeking to understand the health issues which ultimately result if protein fold goes awry as well as protein biology. The broad world of proteins, using its great assortment of shapes, bestows cells with capacities that allow for life to exist and allow for its diversity (e.g., the differences between eye, skin, lung or heart cells, and also the differences between species). But perhaps this is one of the many reasons why the word “protein” comes from the Greek word “protas,” meaning “of primary significance” and indeed they seem to be.  


Protein folding is a complex, physiochemical process by which a protein “folds” or assumes a functional shape to be able to perform their biological function. Proteins are nutrients we obtain from the food we eat and they are considered to be one of the main components of muscles, however, proteins play a wide variety of fundamental roles in the human body. According to research studies, protein misfolding can cause a variety of health issues, including neurological diseases. – Dr. Alex Jimenez D.C., C.C.S.T. Insight



Diet and Exercise for Neurological Disease




The purpose of the article above is to describe protein folding and how it’s associated with neurological diseases. Neurological diseases are associated with the brain, the spine, and the nerves. The scope of our information is limited to chiropractic, musculoskeletal and nervous health issues as well as functional medicine articles, topics, and discussions. To further discuss the subject matter above, please feel free to ask Dr. Alex Jimenez or contact us at 915-850-0900 .  


Curated by Dr. Alex Jimenez  



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