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10.1016/j.jmb.2016.10.017 http://scihub22266oqcxt.onion/10.1016/j.jmb.2016.10.017 C5661953!5661953!27751724     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Biol 2016 ; 428 (23): 4723-35 Nephropedia Template TP {{tp|p=27751724|t=2016. Structural dynamics in Ras and related proteins upon nucleotide switching |pdf=|usr=}}{{27751724}} gab.com Text Structural dynamics in Ras and related proteins upon nucleotide switching JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=27751724 #FOAvip Structural dynamics of Ras proteins contribute to their activity in signal transduction cascades. Directly targeting Ras proteins with small molecules may rely on movement of a conserved structural motif, switch II. To understand Ras signaling and advance Ras targeting strategies, experimental methods to measure Ras dynamics are required. Here we demonstrate the utility of hydrogen-deuterium exchange mass spectrometry to measure Ras dynamics by studying representatives from two branches of the Ras superfamily, Ras and Rho. A comparison of differential deuterium exchange between active (GMPPNP-bound) and inactive (GDP-bound) proteins revealed differences between the families, with the most notable differences occurring in the phosphate-binding loop and switch II. The P-loop exchange signature correlated with switch II dynamics observed in molecular dynamics simulations focused on measuring main chain movement. Hydrogen-deuterium exchange provides a means of evaluating Ras protein dynamics which may be useful for understanding mechanisms of Ras signaling, including activated signaling of pathologic mutants, and for targeting strategies that rely on protein dynamics. Twit Text FOAVip Structural dynamics in Ras and related proteins upon nucleotide switching ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=27751724 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27751724 #FOAvip English Wikipedia <ref>{{Cite pmid|27751724}}</ref> Structural dynamics in Ras and related proteins upon nucleotide switching #MMPMID27751724 Harrison RA; Lu J; Carrasco M; Hunter J; Manandhar A; Gondi S; Westover KD; Engen JR J Mol Biol 2016[Nov]; 428 (23): 4723-35 PMID27751724show ga Structural dynamics of Ras proteins contribute to their activity in signal transduction cascades. Directly targeting Ras proteins with small molecules may rely on movement of a conserved structural motif, switch II. To understand Ras signaling and advance Ras targeting strategies, experimental methods to measure Ras dynamics are required. Here we demonstrate the utility of hydrogen-deuterium exchange mass spectrometry to measure Ras dynamics by studying representatives from two branches of the Ras superfamily, Ras and Rho. A comparison of differential deuterium exchange between active (GMPPNP-bound) and inactive (GDP-bound) proteins revealed differences between the families, with the most notable differences occurring in the phosphate-binding loop and switch II. The P-loop exchange signature correlated with switch II dynamics observed in molecular dynamics simulations focused on measuring main chain movement. Hydrogen-deuterium exchange provides a means of evaluating Ras protein dynamics which may be useful for understanding mechanisms of Ras signaling, including activated signaling of pathologic mutants, and for targeting strategies that rely on protein dynamics. äStructural dynamics in Ras and related proteins upon nucleotide switch(epmc).pdf DeepDyve Pubget Overpricing