Regensburg 2010 – scientific programme
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BP: Fachverband Biologische Physik
BP 14: Evolutionary Game Theory III (joint SOE, BP)
BP 14.2: Talk
Tuesday, March 23, 2010, 14:30–14:45, H44
Predicting correlated mutations of amino acids from protein structure — •Jonas Minning1, Ugo Bastolla2, and Markus Porto1 — 1Technische Universität, Darmstadt, Germany — 2Centro di Biología Molecular, ’Severo Ochoa’, CSIC-UAM, Madrid, Spain
Even though the average sequence similarity for homologous proteins sharing the same fold can reach the threshold of randomness, amino acid sequences maintain the fingerprint of selective pressures on structure and function. We have previously developed an analytical method for computing the probability to observe a given amino acid at a given site in a protein with known native structure, based on an independent site approximation of protein evolution subject to selective constraints on unfolding and misfolding stabilities [1]. However, substitutions at different sites are known to be correlated, and these correlated mutations may give important information for reconstructing native contacts, protein interaction interfaces, or clusters of functionally important residues. Here, we present a model which allows to quantitatively predict the correlated mutations that arise from selective constraints on unfolding and misfolding stabilities. Our model is verified against simulated data of protein sequence evolution and statistical data of proteins in the Protein Databank.
[1] U. Bastolla et al., Proteins 73, 872 (2008).