BeAtMuSiC protocols

BeAtMuSiC specifications

Information


Unique identifier OMICS_11225
Name BeAtMuSiC
Interface Web user interface
Restrictions to use None
Input data The main input of the webserver is the structure of the protein–protein complex, in PDB format. The user may either upload his own structure file, or provide the 4-letter PDB code of the structure, which will then be automatically downloaded from the Protein Data Bank.
Output data The main output of the webserver is the change in binding free energy resulting from each mutation. The webserver also reports the solvent accessibility of the mutated residue, in the complex and in the individual partners. The results may be downloaded as a plain text file, or browsed interactively on the website.
Computer skills Basic
Version 1.0
Stability Stable
Maintained Yes

Maintainer


  • person_outline Yves Dehouck <>

Publication for BeAtMuSiC

BeAtMuSiC IN pipelines

 (3)
2014
PMCID: 3985714
PMID: 24803870
DOI: 10.1021/ct401022c

[…] with experimental values. to calculate binding energy by foldx, we used eq 2 and calculated the unfolding free energy of the whole complex and each monomer separately., the second method, beatmusic21 is specifically trained to calculate the change in binding affinity produced by single missense mutations. it uses residue based statistical potentials that were previously optimized […]

2014
PMCID: 3985714
PMID: 24803870
DOI: 10.1021/ct401022c

[…] in binding affinity produced by single missense mutations. it uses residue based statistical potentials that were previously optimized to discriminate native from decoy complexes.58 in addition, the beatmusic energy function has terms accounting for packing defects and for the effect of mutations on the unfolding free energy of the whole complex in cases where unbound monomers could […]

2014
PMCID: 3985714
PMID: 24803870
DOI: 10.1021/ct401022c

[…] function has terms accounting for packing defects and for the effect of mutations on the unfolding free energy of the whole complex in cases where unbound monomers could be considered disordered. beatmusic is not designed to estimate changes in binding energy for multiple mutations. the third method, cc/pbsa,22 applies the concoord approach to sample the protein configurational ensemble […]

BeAtMuSiC institution(s)
Department of BioModelling, BioInformatics and BioProcesses, Université Libre de Bruxelles (ULB), Brussels, Belgium
BeAtMuSiC funding source(s)
Belgian Fonds de la Recherche Scientifique (F.R.S.-FNRS) through an FRFC grant

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