Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM052018-02
Application #
2190865
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1995-01-01
Project End
1998-12-31
Budget Start
1996-01-01
Budget End
1996-12-31
Support Year
2
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Columbia University (N.Y.)
Department
Chemistry
Type
Other Domestic Higher Education
DUNS #
064931884
City
New York
State
NY
Country
United States
Zip Code
10027
Wang, Lingle; Berne, B J; Friesner, Richard A (2012) On achieving high accuracy and reliability in the calculation of relative protein-ligand binding affinities. Proc Natl Acad Sci U S A 109:1937-42
Zhao, Suwen; Zhu, Kai; Li, Jianing et al. (2011) Progress in super long loop prediction. Proteins 79:2920-35
Abel, Robert; Wang, Lingle; Friesner, Richard A et al. (2010) A displaced-solvent functional analysis of model hydrophobic enclosures. J Chem Theory Comput 6:2924-2934
Trbovic, Nikola; Cho, Jae-Hyun; Abel, Robert et al. (2009) Protein side-chain dynamics and residual conformational entropy. J Am Chem Soc 131:615-22
Abel, Robert; Young, Tom; Farid, Ramy et al. (2008) Role of the active-site solvent in the thermodynamics of factor Xa ligand binding. J Am Chem Soc 130:2817-31
Trbovic, Nikola; Kim, Byungchan; Friesner, Richard A et al. (2008) Structural analysis of protein dynamics by MD simulations and NMR spin-relaxation. Proteins 71:684-94
Felts, Anthony K; Gallicchio, Emilio; Chekmarev, Dmitriy et al. (2008) Prediction of Protein Loop Conformations using the AGBNP Implicit Solvent Model and Torsion Angle Sampling. J Chem Theory Comput 4:855-868
Hagen, Morten; Kim, Byungchan; Liu, Pu et al. (2007) Serial replica exchange. J Phys Chem B 111:1416-23
Xiang, Zhexin; Steinbach, Peter J; Jacobson, Matthew P et al. (2007) Prediction of side-chain conformations on protein surfaces. Proteins 66:814-23
Huang, Xuhui; Hagen, Morten; Kim, Byungchan et al. (2007) Replica exchange with solute tempering: efficiency in large scale systems. J Phys Chem B 111:5405-10

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