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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Univ Calif Santa Barbara, Dept Math, Santa Barbara, CA 93106 USAUniv Calif Santa Barbara, Dept Math, Santa Barbara, CA 93106 USA
Millett, Kenneth C.
Rawdon, Eric J.
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Univ St Thomas, Dept Math, St Paul, MN 55105 USAUniv Calif Santa Barbara, Dept Math, Santa Barbara, CA 93106 USA
Rawdon, Eric J.
Stasiak, Andrzej
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Univ Lausanne, Ctr Integrat Genom, CH-1015 Lausanne, SwitzerlandUniv Calif Santa Barbara, Dept Math, Santa Barbara, CA 93106 USA
Stasiak, Andrzej
Sulkowska, Joanna I.
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Univ Calif San Diego, Ctr Theoret Biol Phys, San Diego, CA 92037 USA
Univ Warsaw, Fac Chem, PL-02093 Warsaw, PolandUniv Calif Santa Barbara, Dept Math, Santa Barbara, CA 93106 USA