The proposed research will investigate the dynamics of hemoglobin using time-resolved spectroscopies and computer modeling in order to help determine the molecular mechanism of cooperativity in oxygen binding. This knowledge was intended to be useful for understanding and developing treatments for hemoglobin disorders, for aiding in the design of blood substitutes, and for the understanding of allosteric proteins in general. Important molecular interactions involved in the R to T transition of hemoglobin will be probed using both transient ultraviolet resonance Raman and Fourier transform spectroscopies. The structural information available from the experimental studies will then be used as constraints in various computer simulations aimed at determining intermediate structures and the dynamics of the R to T transition.

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
5F32HL009322-03
Application #
2459900
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1997-08-01
Project End
Budget Start
1997-08-01
Budget End
1998-08-29
Support Year
3
Fiscal Year
1997
Total Cost
Indirect Cost
Name
Princeton University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
002484665
City
Princeton
State
NJ
Country
United States
Zip Code
08544