The sum of the biological reactions and processes within an organism is effected by proteins, or complexes of proteins with other biomolecules. Determination of a protein's three dimensional structure or fold, is fundamental to elucidating biological form and function. A detailed description of the folding process, the energetics of folding, and the energetics of protein - biomolecule interactions provides valuable insight in understanding the molecular bases of diseases caused by mutant proteins with aberrant functions, and the design of potential targets and gene therapies. There is a large body of evidence which indicates that changes in the hydration state of a protein is a key determinant of the folding process. Using Staphylococcal nuclease as a model system, I propose to study hydration-driven structural changes via a new high pressure X-ray crystallographic technique, and fluorescence and NMR spectroscopy.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Predoctoral Individual National Research Service Award (F31)
Project #
5F31GM064004-03
Application #
6658230
Study Section
Special Emphasis Panel (ZRG1-BIOL-1 (01))
Program Officer
Toliver, Adolphus
Project Start
2002-09-01
Project End
Budget Start
2003-09-01
Budget End
2004-08-31
Support Year
3
Fiscal Year
2003
Total Cost
$40,163
Indirect Cost
Name
Johns Hopkins University
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
001910777
City
Baltimore
State
MD
Country
United States
Zip Code
21218