Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM037123-01
Application #
3292167
Study Section
Biophysics and Biophysical Chemistry A Study Section (BBCA)
Project Start
1985-11-01
Project End
1988-07-31
Budget Start
1985-11-01
Budget End
1986-07-31
Support Year
1
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Michigan Ann Arbor
Department
Type
Schools of Pharmacy
DUNS #
791277940
City
Ann Arbor
State
MI
Country
United States
Zip Code
48109

  Publications

Maiorov, V N; Crippen, G M (1994) Significance of root-mean-square deviation in comparing three-dimensional structures of globular proteins. J Mol Biol 235:625-34
Maiorov, V N; Crippen, G M (1994) Learning about protein folding via potential functions. Proteins 20:167-73
Srivastava, S; Crippen, G M (1993) Analysis of cocaine receptor site ligand binding by three-dimensional Voronoi site modeling approach. J Med Chem 36:3572-9
Bradley, M P; Crippen, G M (1993) Voronoi modeling: the binding of triazines and pyrimidines to L. casei dihydrofolate reductase. J Med Chem 36:3171-7
Maiorov, V N; Crippen, G M (1992) Contact potential that recognizes the correct folding of globular proteins. J Mol Biol 227:876-88
Smellie, A S; Crippen, G M; Richards, W G (1991) Fast drug-receptor mapping by site-directed distances: a novel method of predicting new pharmacological leads. J Chem Inf Comput Sci 31:386-92
Crippen, G M (1991) Prediction of protein folding from amino acid sequence over discrete conformation spaces. Biochemistry 30:4232-7
Crippen, G M (1991) Voronoi binding site models. NIDA Res Monogr 112:7-20
Crippen, G M; Snow, M E (1990) A 1.8 A resolution potential function for protein folding. Biopolymers 29:1479-89
Boulu, L G; Crippen, G M; Barton, H A et al. (1990) Voronoi binding site model of a polycyclic aromatic hydrocarbon binding protein. J Med Chem 33:771-5

Showing the most recent 10 out of 15 publications