The goal of this project is to use site-specific quantitative techniques that have been recently developed in the field of infrared spectroscopy to address several fundamental questions about the alpha-helix-random coil transition as it occurs in short peptides. These questions have become the subject of intense debate in recent years and are relevant to our understanding of early events in protein folding pathways. These issues are also important for understanding the factors that stabilize alpha-helices in peptide hormones and antigens as well as larger systems such as enzymes, antibodies and structural proteins. We intend to directly measure the equilibrium constant(s) for the recruitment of amino acids into propagating alpha-helices and examine how these propensities are modulated by a variety of factors, including sequence-specific interactions, solvent effects and intermolecular interactions. We also intend to examine the thermodynamic parameters that are the basis for differing propagation propensities, and investigate the extent of cooperativity that occurs in helix-coil transitions in short peptide sequences.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM047930-04
Application #
2185358
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1992-08-05
Project End
1996-07-31
Budget Start
1995-01-01
Budget End
1996-07-31
Support Year
4
Fiscal Year
1994
Total Cost
Indirect Cost
Name
San Diego State University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
073371346
City
San Diego
State
CA
Country
United States
Zip Code
92182