This research is aimed at elucidating the minimum set of interactions required to stabilize folded and partially folded protein domains. Attention will be focused on the molten globule state of alpha- lactalbumin, by preparing peptide models of critical regions of this protein and by developing novel techniques for probing long range interactions in partially folded proteins. These experiments will make use of stable spin labels and 2D NMR. These studies of partially folded states will be complemented by determining the interactions required to specify a unique folded structure in a novel three helix """"""""mini-domain"""""""", the E3/E1p domain of a B. Stearothermophilus protein.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
First Independent Research Support & Transition (FIRST) Awards (R29)
Project #
5R29GM054233-04
Application #
2910247
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1996-05-01
Project End
2001-04-30
Budget Start
1999-05-01
Budget End
2000-04-30
Support Year
4
Fiscal Year
1999
Total Cost
Indirect Cost
Name
State University New York Stony Brook
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
804878247
City
Stony Brook
State
NY
Country
United States
Zip Code
11794