title: BeAtMuSiC: Prediction of changes in protein-protein binding affinity on mutations.
abstract: The ability of proteins to establish highly selective interactions with a variety of (macro)molecular partners is a crucial prerequisite to the realization of their biological functions. The availability of computational tools to evaluate the impact of mutations on protein-protein binding can therefore be valuable in a wide range of industrial and biomedical applications, and help rationalize the consequences of non-synonymous single-nucleotide polymorphisms. BeAtMuSiC (http://babylone.ulb.ac.be/beatmusic) is a coarse-grained predictor of the changes in binding free energy induced by point mutations. It relies on a set of statistical potentials derived from known protein structures, and combines the effect of the mutation on the strength of the interactions at the interface, and on the overall stability of the complex. The BeAtMuSiC server requires as input the structure of the protein-protein complex, and gives the possibility to assess rapidly all possible mutations in a protein chain or at the interface, with predictive performances that are in line with the best current methodologies.
authors.affiliation: Department of BioModelling, BioInformatics and BioProcesses, Université Libre de Bruxelles, CP165/61, Av. Fr. Roosevelt 50, 1050 Brussels, Belgium. ydehouck@ulb.ac.be
authors.forename: Yves
authors.initials: Y
authors.lastname: Dehouck
authors.forename: Jean Marc
authors.initials: JM
authors.lastname: Kwasigroch
authors.forename: Marianne
authors.initials: M
authors.lastname: Rooman
authors.forename: Dimitri
authors.initials: D
authors.lastname: Gilis
mesh_terms: D020407:Internet; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D011485:Protein Binding; D017510:Protein Folding; D012984:Software
chemical_list: D046912:Multiprotein Complexes