Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM041371-08
Application #
2180836
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1988-12-01
Project End
1997-11-30
Budget Start
1995-12-01
Budget End
1996-11-30
Support Year
8
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Columbia University (N.Y.)
Department
Biochemistry
Type
Schools of Medicine
DUNS #
167204994
City
New York
State
NY
Country
United States
Zip Code
10032
Petrey, D; Honig, B (2000) Free energy determinants of tertiary structure and the evaluation of protein models. Protein Sci 9:2181-91
Norel, R; Petrey, D; Wolfson, H J et al. (1999) Examination of shape complementarity in docking of unbound proteins. Proteins 36:307-17
Abramovitz, D L; Friedman, R A; Pyle, A M (1996) Catalytic role of 2'-hydroxyl groups within a group II intron active site. Science 271:1410-3
Misra, V K; Honig, B (1996) The electrostatic contribution to the B to Z transition of DNA. Biochemistry 35:1115-24
Collini, M; Chirico, G; Baldini, G et al. (1995) Conformation of short DNA fragments by modulated fluorescence polarization anisotropy. Biopolymers 36:211-25
Friedman, R A; Honig, B (1995) A free energy analysis of nucleic acid base stacking in aqueous solution. Biophys J 69:1528-35
Misra, V K; Honig, B (1995) On the magnitude of the electrostatic contribution to ligand-DNA interactions. Proc Natl Acad Sci U S A 92:4691-5
Honig, B; Nicholls, A (1995) Classical electrostatics in biology and chemistry. Science 268:1144-9
Sharp, K A; Friedman, R A; Misra, V et al. (1995) Salt effects on polyelectrolyte-ligand binding: comparison of Poisson-Boltzmann, and limiting law/counterion binding models. Biopolymers 36:245-62
Misra, V K; Hecht, J L; Sharp, K A et al. (1994) Salt effects on protein-DNA interactions. The lambda cI repressor and EcoRI endonuclease. J Mol Biol 238:264-80

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