Pressure Studies of Protein Dynamics
Final rept. 1 Mar 1989-28 Feb 1992
ILLINOIS UNIV AT URBANA LOOMIS LAB OF PHYSICS
Pagination or Media Count:
Our goal is a quantitative understanding of the relation between protein structure, motions, and function. We attack four related objectives 1 exploration of the structure and organization of the energy landscape of proteins 2 Investigation of protein motions on the energy landscape 3 study of the dependence of the energy landscape and protein motions on external agents 4 elucidation of the connection between protein motions and biological function. We study protein dynamics and function by combining two techniques flash photolysis and optical spectroscopy from the ultraviolet to the mid- infrared including FTIR spectroscopy. We measure protein spectra, relaxations, and reactions over wide ranges in temperature 10-330K, time ns-ks, pressure 0.2-400 MPa, solvent conditions and pH. Pressure is a crucial variable both as static parameter and perturbation to induce protein relaxations. Myoglobin is used as prototypical protein to explore concepts and laws that are the generalized to other more complicated heme protein. We then are able to extract protein specific behavior and refine the basic concepts and laws.
- Physical Chemistry