Templates for Protein Secondary Structures (Chemistry)
{'Code': '03090003', 'Directorate': {'LongName': 'Direct For Mathematical & Physical Scien'}, 'Division': {'LongName': 'Division Of Chemistry'}}
{'SignBlockName': 'John S. Showell'}
Dr. Kemp has a pioneering program in construction of small                      molecule models that permit better understanding of the chemistry               and structure of peptides and proteins.  This project, which is                 in the Organic and Macromolecular Chemistry Program, should lead                to  better understanding of biological interactions at the                      molecular level which could lead to very important industrial                   consequences.                                                                                                                                                   Current theories of protein folding postulate that regions in the               amino acid sequence that have a high probability of assuming                    specific secondary structures act as nucleation sites for further               folding.  Moreover, many interactions of receptors with peptide                 hormones or proteins with posttranslational modifying enzymes                   appear to involve beta-turns at the site of recognition.  In this               work, analogs of amino acids are to be synthesized which are more               rigid than the natural amino acids and which stabilize the                      several types of turns, pleated sheets and alpha-helices when                   attached to peptide chains.  The emphasis is on demonstrating                   that the turn, sheet, and helix templates that have been prepared               actually assume the proposed structures when attached to simple                 peptides.  A variety of tests for conformations of these simple                 hybrids are proposed to establish this latter point.  Second                    generation templates that can be used to test further hypotheses                will be synthesized and studied.                                                                                                                                In subsequent studies the proven templates for secondary                        structure are to be incorporated semisynthetically into proteins                at key folding regions.  In a related effort, analogs of some of                the peptide hormones are to be prepared, using the turn-templates               as structural elements.  With these studies, the object is to                   enhance the binding at the receptor site as well as to protect                  the hormone analog from proteolysis.  The long-range objectives                 of this study are thus the construction of hybrid peptides and                  proteins with properties that are not realizable with the natural               amino acids.
{'FirstName': 'Daniel', 'LastName': 'Kemp', 'EmailAddress': 'kemp@mit.edu', 'StartDate': '07/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Massachusetts Institute of Technology', 'CityName': 'Cambridge', 'ZipCode': '021394301', 'PhoneNumber': '6172531000', 'StreetAddress': '77 MASSACHUSETTS AVE', 'CountryName': 'United States', 'StateName': 'Massachusetts', 'StateCode': 'MA'}
{'Code': '1948', 'Text': 'SYNTHESIS'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8701110.xml'}