Proteins Structure Function and Bioinformatics · 2004 · 273 citations · 47 references
Life SciencesBioinformaticsBiophysicsComputational ChemistryStructural BiologyStructural BiophysicsComputational Structural BiologyEnergy MinimizationMacromolecular Structure DeterminationMolecular DynamicsProtein StructureProtein Structure ModelingDecoy SetsGeneralized Born ModelsMolecular Dynamics Of ProteinsProtein Decoy SelectionProtein Energy MinimizationProtein Structure AnalysisProtein Structure AssessmentScoring Functions
Recent works have shown the ability of physics-based potentials (e.g., CHARMM and OPLS-AA) and energy minimization to differentiate the native protein structures from large ensemble of non-native structures. In this study, we extended previous work by other authors and developed an energy scoring function using a new set of AMBER parameters (also recently developed in our laboratory) in conjunction with molecular dynamics and the Generalized Born solvent model. We evaluated the performance of our new scoring function by examining its ability to distinguish between the native and decoy protein structures. Here we present a systematic comparison of our results with those obtained with use of other physics-based potentials by previous authors. A total of 7 decoy sets, 117 protein sequences, and more than 41,000 structures were evaluated. The results of our study showed that our new scoring function represents a significant improvement over previously published physics-based scoring functions.
47
Molecular dynamics with coupling to an external bath
Herman J. C. Berendsen, Johan P. M. Postma, Wilfred F. van Gunsteren et al. · The Journal of Chemical Physics · 1984 · 31K citations · Full text
Natural Sciences, Chemistry, Physics +17
Principles that Govern the Folding of Protein Chains
Christian B. Anfinsen · Science · 1973 · 7.1K citations