Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.bpj.2015.06.004 http://scihub22266oqcxt.onion/10.1016/j.bpj.2015.06.004 C4576147!4576147!26143655     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2015 ; 109 (6): 1101-9 Nephropedia Template TP {{tp|p=26143655|t=2015. Structure-Encoded Global Motions and Their Role in Mediating Protein-Substrate Interactions |pdf=|usr=}}{{26143655}} gab.com Text Structure-Encoded Global Motions and Their Role in Mediating Protein-Substrate Interactions JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=26143655 #FOAvip Recent structure-based computational studies suggest that, in contrast to the classical description of equilibrium fluctuations as wigglings and jigglings, proteins have access to well-defined spectra of collective motions, called intrinsic dynamics, encoded by their structure under native state conditions. In particular, the global modes of motions (at the low frequency end of the spectrum) are shown by multiple studies to be highly robust to minor differences in the structure or to detailed interactions at the atomic level. These modes, encoded by the overall fold, usually define the mechanisms of interactions with substrates. They can be estimated by low-resolution models such as the elastic network models (ENMs) exclusively based on interresidue contact topology. The ability of ENMs to efficiently assess the global motions intrinsically favored by the overall fold as well as the relevance of these predictions to the dominant changes in structure experimentally observed for a given protein in the presence of different substrates suggest that the intrinsic dynamics plays a role in mediating protein-substrate interactions. These observations underscore the functional significance of structure-encoded dynamics, or the importance of the predisposition to favor functional global modes in the evolutionary selection of structures. Twit Text FOAVip Structure-Encoded Global Motions and Their Role in Mediating Protein-Substrate Interactions ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=26143655 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26143655 #FOAvip English Wikipedia <ref>{{Cite pmid|26143655}}</ref> Structure-Encoded Global Motions and Their Role in Mediating Protein-Substrate Interactions #MMPMID26143655 Bahar I; Cheng M; Lee J; Kaya C; Zhang S Biophys J 2015[Sep]; 109 (6): 1101-9 PMID26143655show ga Recent structure-based computational studies suggest that, in contrast to the classical description of equilibrium fluctuations as wigglings and jigglings, proteins have access to well-defined spectra of collective motions, called intrinsic dynamics, encoded by their structure under native state conditions. In particular, the global modes of motions (at the low frequency end of the spectrum) are shown by multiple studies to be highly robust to minor differences in the structure or to detailed interactions at the atomic level. These modes, encoded by the overall fold, usually define the mechanisms of interactions with substrates. They can be estimated by low-resolution models such as the elastic network models (ENMs) exclusively based on interresidue contact topology. The ability of ENMs to efficiently assess the global motions intrinsically favored by the overall fold as well as the relevance of these predictions to the dominant changes in structure experimentally observed for a given protein in the presence of different substrates suggest that the intrinsic dynamics plays a role in mediating protein-substrate interactions. These observations underscore the functional significance of structure-encoded dynamics, or the importance of the predisposition to favor functional global modes in the evolutionary selection of structures. äStructure-Encoded Global Motions and Their Role in Mediating Protein-S(epmc).pdf DeepDyve Pubget Overpricing