Thermal fluctuations create regional disorder within protein structures. It is increasingly apparent that this dynamical disorder is both intrinsic to proteins and inherently important for their functioning. Dr. Friedman proposes to study this relationship between dynamical disorder and functionality. He will use heme proteins as a model system, studying the rebinding of ligands after photodissication. The focus will be upon characterization of parameters of the disordered states and establishing their relationship to the quantum yield of photolysis, the rebinding rates and the entry into and escape from the heme pocket by the ligand.

Agency
National Science Foundation (NSF)
Institute
Division of Molecular and Cellular Biosciences (MCB)
Application #
9005697
Program Officer
Arthur Kowalsky
Project Start
Project End
Budget Start
1990-09-01
Budget End
1993-05-31
Support Year
Fiscal Year
1990
Total Cost
$281,250
Indirect Cost
Name
New York University
Department
Type
DUNS #
City
New York
State
NY
Country
United States
Zip Code
10012