TAILIEUCHUNG - Báo cáo sinh học: " Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins"

Tuyển tập các báo cáo nghiên cứu về sinh học được đăng trên tạp chí sinh học Journal of Biology đề tài: Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins. | Journal of Biology BioMed Central Minireview Liaison amid disorder non-native interactions may underpin long-range coupling in proteins Hue Sun Chan and Zhuqing Zhang Address Department of Biochemistry Department of Molecular Genetics and Department of Physics University of Toronto 1 King s College Circle MSB 5207 Toronto Ontario M5S 1A8 Canada. Correspondence Hue Sun Chan. Email chan@ Published 13 March 2009 Journal of Biology 2009 8 27 doi jbiol126 The electronic version of this article is the complete one and can be found online at http content 8 3 27 2009 BioMed Central Ltd Abstract A lattice-model study of double-mutant cycles published in BMC Structural Biology underscores how interactions in non-native conformations can lead to thermodynamic coupling between distant residues in globular proteins adding to recent advances in delineating the often crucial roles played by disordered conformational ensembles in protein behavior. How do the conformational structures dynamics and biological function of a protein emerge from the interactions among its amino acid residues A significant part of current ideas about protein behaviors is based on structures in the Protein Data Bank PDB and notions of contact-like interactions between amino acid residues in spatial proximity. While useful this picture is limited. In particular studies of allostery and mutational analyses have demonstrated that energetic coupling can exist between residues at positions far apart in a protein s native structure. An intriguing possibility is that such apparently long-range coupling may arise from the residues transient association in the unfolded state. This scenario was elucidated by an extensive computational study using two-dimensional lattice protein models published recently in BMC Structural Biology by the groups of Ron Unger and Amnon Horovitz Noivirt-Brik et al. 1 . Their study provides a theoretical framework that will be useful for .

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