SRide: a server for identifying stabilizing residues in proteins | Zendy

Csaba Magyar | Zendy; M. Michael Gromiha | Zendy; Gerard Pujadas | Zendy; Gábor Tusnády | Zendy; István Simon | Zendy

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SRide: a server for identifying stabilizing residues in proteins

Author(s) -

Csaba Magyar,

M. Michael Gromiha,

Gerard Pujadas,

Gábor Tusnády,

István Simon

Publication year - 2005

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gki409

Subject(s) - biology , residue (chemistry) , computational biology , homology modeling , homology (biology) , protein engineering , protein structure , conserved sequence , biochemistry , bioinformatics , peptide sequence , amino acid , enzyme , gene

Residues expected to play key roles in the stabilization of proteins [stabilizing residues (SRs)] are selected by combining several methods based mainly on the interactions of a given residue with its spatial, rather than its sequential neighborhood and by considering the evolutionary conservation of the residues. A residue is selected as a stabilizing residue if it has high surrounding hydrophobicity, high long-range order, high conservation score and if it belongs to a stabilization center. The definition of all these parameters and the thresholds used to identify the SRs are discussed in detail. The algorithm for identifying SRs was originally developed for TIM-barrel proteins [M. M. Gromiha, G. Pujadas, C. Magyar, S. Selvaraj, and I. Simon (2004), Proteins, 55, 316-329] and is now generalized for all proteins of known 3D structure. SRs could be applied in protein engineering and homology modeling and could also help to explain certain folds with significant stability. The SRide server is located at http://sride.enzim.hu.

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