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Vol 47(2013) N 1 p. 149-160; G.V. Novikov1, V.S. Sivozhelezov1*, K.V. Shaitan 2 Functionally Relevant Conformational Dynamics of Water-Soluble Proteins 1Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia2Department of Biology, Moscow State University, Moscow, 119991 Russia *vsivo00@gmail.com Received - 2012-06-24; Accepted - 2012-07-25 A study of the functional-relevant dynamics of three typical water-soluble proteins, including Calmodulin, Src-tyrosine kinase, and a repressor of the trip operon, has been reported. The application of state-of-art methods of structural bioinformatics allowed us to identify the dynamics seen in the X-ray structures of the investigated proteins associated with their specific biological functions. In addition, technique of normal mode analysis reveals the most probable directions of the functionally relevant motions for all proteins. Importantly, the overall type of the motions observed in the lowest-frequency modes was very similar to the motions seen from the analysis of the X-ray data of the examined macromolecules. Thus, it was shown that the large-scale, as well as local, conformational motions of the proteins might already be predetermined at the level of their tertiary structures. In particular, the determining factor might be the specific fold of the α-helices. Thus, the functionally relevant in vivo dynamics of the investigated proteins might be evolutionarily formed by natural selection at the level of the spatial topology. dynamics, conformation, α-helix, water-soluble proteins, calmodulin, kinases, repressor, X-ray crystallography, structural bioinformatics |