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10.1021/acs.jpcb.6b03199 http://scihub22266oqcxt.onion/10.1021/acs.jpcb.6b03199 C4911233!4911233!27183318     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Phys+Chem+B 2016 ; 120 (23): 5103-13 Nephropedia Template TP {{tp|p=27183318|t=2016. Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function |pdf=|usr=}}{{27183318}} gab.com Text Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function JO: J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=27183318 #FOAvip While folding or performing functions, a protein can sample a rich set of conformational space. However, experimentally capturing all of the important motions with sufficient detail to allow a mechanistic description of their dynamics is nontrivial since such conformational events often occur over a wide range of time and length scales. Therefore, many methods have been employed to assess protein conformational dynamics and, depending on the nature of the conformational transition in question, some may be more advantageous than others. Herein, we describe our recent efforts, and also those of others, wherever appropriate, to use infrared- and fluorescence-based techniques to interrogate protein folding and functional dynamics. Specifically, we focus on discussing how to use extrinsic spectroscopic probes to enhance the structural resolution of these techniques and how to exploit various cross-linking strategies to acquire dynamic and mechanistic information that was previously difficult to attain. Twit Text FOAVip Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function ????J Phys Chem B http://www.kidney.de/pget.php?&tw=1&pmid=27183318 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27183318 #FOAvip English Wikipedia <ref>{{Cite pmid|27183318}}</ref> Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function #MMPMID27183318 Ding B; Hilaire MR; Gai F J Phys Chem B 2016[Jun]; 120 (23): 5103-13 PMID27183318show ga While folding or performing functions, a protein can sample a rich set of conformational space. However, experimentally capturing all of the important motions with sufficient detail to allow a mechanistic description of their dynamics is nontrivial since such conformational events often occur over a wide range of time and length scales. Therefore, many methods have been employed to assess protein conformational dynamics and, depending on the nature of the conformational transition in question, some may be more advantageous than others. Herein, we describe our recent efforts, and also those of others, wherever appropriate, to use infrared- and fluorescence-based techniques to interrogate protein folding and functional dynamics. Specifically, we focus on discussing how to use extrinsic spectroscopic probes to enhance the structural resolution of these techniques and how to exploit various cross-linking strategies to acquire dynamic and mechanistic information that was previously difficult to attain. äInfrared and Fluorescence Assessment of Protein Dynamics: From Folding(epmc).pdf DeepDyve Pubget Overpricing