ELASPIC web-server: proteome-wide structure-based prediction of mutation effects on protein stability and binding affinity
Author(s) -
Daniel Witvliet,
Alexey Strokach,
Andrés Felipe Giraldo-Forero,
Joan Teyra,
Recep Çolak,
Philip M. Kim
Publication year - 2016
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btw031
Subject(s) - uniprot , web server , computer science , proteome , computational biology , protein domain , domain (mathematical analysis) , homology modeling , bioinformatics , biology , genetics , the internet , world wide web , mathematics , mathematical analysis , biochemistry , gene , enzyme
ELASPIC is a novel ensemble machine-learning approach that predicts the effects of mutations on protein folding and protein-protein interactions. Here, we present the ELASPIC webserver, which makes the ELASPIC pipeline available through a fast and intuitive interface. The webserver can be used to evaluate the effect of mutations on any protein in the Uniprot database, and allows all predicted results, including modeled wild-type and mutated structures, to be managed and viewed online and downloaded if needed. It is backed by a database which contains improved structural domain definitions, and a list of curated domain-domain interactions for all known proteins, as well as homology models of domains and domain-domain interactions for the human proteome. Homology models for proteins of other organisms are calculated on the fly, and mutations are evaluated within minutes once the homology model is available.
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