RING: networking interacting residues, evolutionary information and energetics in protein structures
نویسندگان
چکیده
منابع مشابه
Inferring repeat-protein energetics from evolutionary information
Natural protein sequences contain a record of their history. A common constraint in a given protein family is the ability to fold to specific structures, and it has been shown possible to infer the main native ensemble by analyzing covariations in extant sequences. Still, many natural proteins that fold into the same structural topology show different stabilization energies, and these are often...
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Key amino acid positions that are important for maintaining the 3D structure of a protein and/or its function(s), e.g. catalytic activity, binding to ligand, DNA or other proteins, are often under strong evolutionary constraints. Thus, the biological importance of a residue often correlates with its level of evolutionary conservation within the protein family. ConSurf (http://consurf.tau.ac.il/...
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It would be great if interface residues, which are responsible for protein-protein interactions, could be determined from the amino acid sequence. Sequence Harmony, Multi-RELIEF, SDPpred and GroupSim+ConsWin are used to predict interface residues from residue conservation between interacting and non-interacting groups. Therefore, a dataset based on Fungal Orthologous Groups is used. Different a...
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ژورنال
عنوان ژورنال: Bioinformatics
سال: 2011
ISSN: 1367-4803,1460-2059
DOI: 10.1093/bioinformatics/btr191