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.

10.1038/srep18128 http://scihub22266oqcxt.onion/10.1038/srep18128 C4676062!4676062!26658321     free     free     free       Sci+Rep 2015 ; 5 (ä): ä Nephropedia Template TP {{tp|p=26658321|t=2015. Intrinsic Localized Modes in Proteins |pdf=|usr=}}{{26658321}} gab.com Text Intrinsic Localized Modes in Proteins JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26658321 #FOAvip Protein dynamics is essential for proteins to function. Here we predicted the existence of rare, large nonlinear excitations, termed intrinsic localized modes (ILMs), of the main chain of proteins based on all-atom molecular dynamics simulations of two fast-folder proteins and of a rigid ?/? protein at 300?K and at 380?K in solution. These nonlinear excitations arise from the anharmonicity of the protein dynamics. The ILMs were detected by computing the Shannon entropy of the protein main-chain fluctuations. In the non-native state (significantly explored at 380?K), the probability of their excitation was increased by a factor between 9 and 28 for the fast-folder proteins and by a factor 2 for the rigid protein. This enhancement in the non-native state was due to glycine, as demonstrated by simulations in which glycine was mutated to alanine. These ILMs might play a functional role in the flexible regions of proteins and in proteins in a non-native state (i.e. misfolded or unfolded states). Twit Text FOAVip Intrinsic Localized Modes in Proteins ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26658321 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26658321 #FOAvip English Wikipedia <ref>{{Cite pmid|26658321}}</ref> Intrinsic Localized Modes in Proteins #MMPMID26658321 Nicolaï A; Delarue P; Senet P Sci Rep 2015[]; 5 (ä): ä PMID26658321show ga Protein dynamics is essential for proteins to function. Here we predicted the existence of rare, large nonlinear excitations, termed intrinsic localized modes (ILMs), of the main chain of proteins based on all-atom molecular dynamics simulations of two fast-folder proteins and of a rigid ?/? protein at 300?K and at 380?K in solution. These nonlinear excitations arise from the anharmonicity of the protein dynamics. The ILMs were detected by computing the Shannon entropy of the protein main-chain fluctuations. In the non-native state (significantly explored at 380?K), the probability of their excitation was increased by a factor between 9 and 28 for the fast-folder proteins and by a factor 2 for the rigid protein. This enhancement in the non-native state was due to glycine, as demonstrated by simulations in which glycine was mutated to alanine. These ILMs might play a functional role in the flexible regions of proteins and in proteins in a non-native state (i.e. misfolded or unfolded states). äIntrinsic Localized Modes in Proteins (epmc).pdf DeepDyve Pubget Overpricing