Theoretical Studies of Membrane Proteins
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Arthur Kowalsky', 'PO_EMAI': None, 'PO_PHON': None}
Theoretical analysis and computer simulations will be used to                   address a number of problems associated with membrane proteins.                 The goals will be to develop insights, computational                            methodologies and models which will facilitate the design and                   interpretation of experiments on membrane proteins in general                   and retinal proteins in particular.  Dr. Honig will focus on                    three general areas:  1) he will address electrostatic questions                with a recently developed method to obtain electrostatic energies               of macromolecular systems; 2) he will develope methods to                       predict amino-acid side-chain conformations and helix-helix                     orientations in membrane proteins; and 3) he will continue                      efforts to understand the structure and function of retinal                     proteins.                                                                                                                                                       In the past few years there has been a large increase in the                    understanding of the structure of membrane proteins.  A                         significant number of amino acid sequences have been reported and               these have revealed remarkable homologies between different                     families of proteins.  Sequence analysis and some structural                    information has suggested that many transmembrane proteins share                common structural elements.  In particular, it appears that alpha               helices are a major structural motif in membrane proteins.  A                   number of laboratories now have the capability of modifying                     proteins essentially at will.  The problem though is what to                    modify.  There is an absence of well-defined testable models, due               in part to uncertainties as to the principles that govern the                   structure and function of membrane proteins.  This project,                     hopefully, should help to overcome this.
{'FirstName': 'Barry', 'LastName': 'Honig', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Barry Honig', 'EmailAddress': 'bh6@columbia.edu', 'NSF_ID': '000157401', 'StartDate': '07/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Columbia University', 'CityName': 'NEW YORK', 'ZipCode': '100277922', 'PhoneNumber': '2128546851', 'StreetAddress': '615 W 131ST ST', 'StreetAddress2': 'MC 8741', 'CountryName': 'United States', 'StateName': 'New York', 'StateCode': 'NY', 'CONGRESSDISTRICT': '13', 'CONGRESS_DISTRICT_ORG': 'NY13', 'ORG_UEI_NUM': 'F4N1QNPB95M4', 'ORG_LGL_BUS_NAME': 'THE TRUSTEES OF COLUMBIA UNIVERSITY IN THE CITY OF NEW YORK', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1164', 'Text': 'MOLECULAR BIOPHYSICS'}
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