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Article

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

PloS one - 1 Jan 2013

Beard Hege, Cholleti Anuradha, Pearlman David, Sherman Woody, Loving Kathryn A

Abstract excerpt

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 to calculate differences in binding free energy between wild type and mutant proteins. Crucially, we made no changes...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 24340062
DOI: 10.1371/journal.pone.0082849
PMCID: PMC3858304

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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