A preference-based free-energy parameterization of enzyme-inhibitor binding. Applications to HIV-1-protease inhibitor design
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Selecting near-native conformations in homology modeling: the role of molecular mechanics and solvation termsQuantitative prediction of protein-protein binding affinity with a potential of mean force considering volume correction.What is the best reference state for designing statistical atomic potentials in protein structure prediction?Towards understanding the mechanisms of molecular recognition by computer simulations of ligand-protein interactions.The dependence of all-atom statistical potentials on structural training database.RNA base-amino acid interaction strengths derived from structures and sequences.A comprehensive examination of the contributions to the binding entropy of protein-ligand complexes.Consistencies of individual DNA base-amino acid interactions in structures and sequencesMolecular docking: a powerful approach for structure-based drug discoveryEvaluation of several two-step scoring functions based on linear interaction energy, effective ligand size, and empirical pair potentials for prediction of protein-ligand binding geometry and free energy.Inclusion of solvation and entropy in the knowledge-based scoring function for protein-ligand interactionsEmpirical free energy calculation: comparison to calorimetric data.Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction.Functional group based Ligand binding affinity scoring function at atomic environmental level.Scoring and lessons learned with the CSAR benchmark using an improved iterative knowledge-based scoring function.Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences.Comparison of binding energies of SrcSH2-phosphotyrosyl peptides with structure-based prediction using surface area based empirical parameterization.Processing multimode binding situations in simulation-based prediction of ligand-macromolecule affinities.Analysis of knowledge-based protein-ligand potentials using a self-consistent method.Computationally accessible method for estimating free energy changes resulting from site-specific mutations of biomolecules: systematic model building and structural/hydropathic analysis of deoxy and oxy hemoglobins.Direct photoaffinity labeling by dolastatin 10 of the amino-terminal peptide of beta-tubulin containing cysteine 12.Scoring docked conformations generated by rigid-body protein-protein docking.Mapping the binding site of colchicinoids on beta -tubulin. 2-Chloroacetyl-2-demethylthiocolchicine covalently reacts predominantly with cysteine 239 and secondarily with cysteine 354.A new method for predicting binding free energy between receptor and ligand.CH···O Hydrogen Bonds at Protein-Protein InterfacesStability scale and atomic solvation parameters extracted from 1023 mutation experiments
P2860
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P2860
A preference-based free-energy parameterization of enzyme-inhibitor binding. Applications to HIV-1-protease inhibitor design
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
A preference-based free-energy ...... IV-1-protease inhibitor design
@ast
A preference-based free-energy ...... IV-1-protease inhibitor design
@en
type
label
A preference-based free-energy ...... IV-1-protease inhibitor design
@ast
A preference-based free-energy ...... IV-1-protease inhibitor design
@en
prefLabel
A preference-based free-energy ...... IV-1-protease inhibitor design
@ast
A preference-based free-energy ...... IV-1-protease inhibitor design
@en
P2093
P2860
P356
P1433
P1476
A preference-based free-energy ...... IV-1-protease inhibitor design
@en
P2093
A Wallqvist
D G Covell
R L Jernigan
P2860
P304
P356
10.1002/PRO.5560040923
P577
1995-09-01T00:00:00Z