Structural Studies of Bacteriorhodopsin
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Kamal Shukla', 'PO_EMAI': None, 'PO_PHON': None}
The hypothesis that transmembrane helices are independently                     stable folding units will be examined by studies of fragments of                bacteriorhodopsin (bR) and intact bR reconstituted in lipid                     vesicles.  The consequences of sequence modifications will be                   studied in a collaborative project with Dr. Khorana at MIT.  The                interaction of fragments with each other will be followed using                 vesicle fusion techniques, neutron and X-ray diffraction                        structural methods, spectroscopic measurements and chemical                     modification techniques.                                                                                                                                        The protein folding problem represents one of the most important                scientific challenges facing biochemists, biophysicists and                     physical chemists as well as the major gap in the understanding                 of the flow of information in living systems.  Understanding the                three-dimensional implications of the linear, abstract                          information in DNA can be regarded as a true understanding of the               genetic code.  Important principles remain to be established and                any attempt to engineer proteins de novo or to understand medical               problems in terms of altered genetic information must benefit                   enormously from insights concerning macromolecular folding.                     However, in spite of the practical importance and intellectual                  fascination of the problem, structural prediction and the                       determination of pathways of folding remain elusive goals.
{'FirstName': 'Donald', 'LastName': 'Engelman', 'PI_MID_INIT': 'M', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Donald M Engelman', 'EmailAddress': 'donald.engelman@yale.edu', 'NSF_ID': '000466937', 'StartDate': '05/16/1994', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Yale University', 'CityName': 'NEW HAVEN', 'ZipCode': '065113572', 'PhoneNumber': '2037854689', 'StreetAddress': '150 MUNSON ST', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Connecticut', 'StateCode': 'CT', 'CONGRESSDISTRICT': '03', 'CONGRESS_DISTRICT_ORG': 'CT03', 'ORG_UEI_NUM': 'FL6GV84CKN57', 'ORG_LGL_BUS_NAME': 'YALE UNIV', 'ORG_PRNT_UEI_NUM': 'FL6GV84CKN57'}
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{'Code': '1164', 'Text': 'MOLECULAR BIOPHYSICS'}
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