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10.1016/j.bpj.2015.08.009 http://scihub22266oqcxt.onion/10.1016/j.bpj.2015.08.009 C4576321!4576321!26338443     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2015 ; 109 (6): 1240-50 Nephropedia Template TP {{tp|p=26338443|t=2015. Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes?|pdf=|usr=}}{{26338443}} gab.com Text Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=26338443 #FOAvip We examine the contrast between mechanisms for allosteric signaling that involve structural change, and those that do not, from the perspective of allosteric pathways. In particular we treat in detail the case of fluctuation-allostery by which amplitude modulation of the thermal fluctuations of the elastic normal modes conveys the allosteric signal, and address the question of what an allosteric pathway means in this case. We find that a perturbation theory of thermal elastic solids and nonperturbative approach (by super-coarse-graining elasticity into internal bending modes) have opposite signatures in their structure of correlated pathways. We illustrate the effect from analysis of previous results from GlxR of Corynebacterium glutamicum, an example of the CRP/FNR transcription family of allosteric homodimers. We find that the visibility of both correlated pathways and disconnected sites of correlated motion in this protein suggests that mechanisms of local elastic stretch and bend are recruited for the purpose of creating and controlling allosteric cooperativity. Twit Text FOAVip Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=26338443 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26338443 #FOAvip English Wikipedia <ref>{{Cite pmid|26338443}}</ref> Dynamic Transmission of Protein Allostery without Structural Change: Spatial Pathways or Global Modes? #MMPMID26338443 McLeish T; Cann M; Rodgers T Biophys J 2015[Sep]; 109 (6): 1240-50 PMID26338443show ga We examine the contrast between mechanisms for allosteric signaling that involve structural change, and those that do not, from the perspective of allosteric pathways. In particular we treat in detail the case of fluctuation-allostery by which amplitude modulation of the thermal fluctuations of the elastic normal modes conveys the allosteric signal, and address the question of what an allosteric pathway means in this case. We find that a perturbation theory of thermal elastic solids and nonperturbative approach (by super-coarse-graining elasticity into internal bending modes) have opposite signatures in their structure of correlated pathways. We illustrate the effect from analysis of previous results from GlxR of Corynebacterium glutamicum, an example of the CRP/FNR transcription family of allosteric homodimers. We find that the visibility of both correlated pathways and disconnected sites of correlated motion in this protein suggests that mechanisms of local elastic stretch and bend are recruited for the purpose of creating and controlling allosteric cooperativity. äDynamic Transmission of Protein Allostery without Structural Change: S(epmc).pdf DeepDyve Pubget Overpricing