Applying physics-based scoring to calculate free energies of binding for single amino acid mutations in protein-protein complexes

Predicting changes in protein binding affinity due to single amino acid mutations helps us better understand the driving forces underlying protein-protein interactions and design improved biotherapeutics. Here, we use the MM-GBSA approach with the OPLS2005 force field and the VSGB2.0 solvent model t...

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Veröffentlicht in:	PloS one 2013-12, Vol.8 (12), p.e82849-e82849
Hauptverfasser:	Beard, Hege, Cholleti, Anuradha, Pearlman, David, Sherman, Woody, Loving, Kathryn A
Format:	Artikel
Sprache:	eng
Schlagworte:	Acids Affinity Algorithms Amino acids Amino Acids - chemistry Analysis Animals Antigens Binding energy Binding sites Biochemistry Bioinformatics Computational Biology - methods Computer Simulation DNA Mutational Analysis Energy (Physics) Enzymes Evaluation Free energy Genetic aspects Humans Hydrogen Bonding Kinases Mathematical models Models, Molecular Mutagenesis Mutation Physics Predictions Protein Binding Protein engineering Protein interaction Protein Interaction Mapping Protein Structure, Secondary Protein-protein interactions Proteins Software Solvents Statistical analysis Thermodynamics
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