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10.1073/pnas.1606610113 http://scihub22266oqcxt.onion/10.1073/pnas.1606610113 C5018803!5018803!27551082     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (36): 10073-8 Nephropedia Template TP {{tp|p=27551082|t=2016. Changes in active site histidine hydrogen bonding trigger cryptochrome activation |pdf=|usr=}}{{27551082}} gab.com Text Changes in active site histidine hydrogen bonding trigger cryptochrome activation JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27551082 #FOAvip There are few detailed mechanistic models that describe how light-sensing proteins convert photochemistry into conformational signals. Combined computational and experimental investigations reveal how photoreduction of the Drosophila cryptochrome (dCRY) flavin induces protonation of a neighboring conserved His residue. Altered His hydrogen bonding then leads to conformational change in a key regulatory element of the protein. These data provide further evidence for involvement of a flavin anionic semiquinone in the dCRY signaling state and allow for the design of variants that can be used to separate dCRY biological functions or as tools for optogenetics. Twit Text FOAVip Changes in active site histidine hydrogen bonding trigger cryptochrome activation ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27551082 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27551082 #FOAvip English Wikipedia <ref>{{Cite pmid|27551082}}</ref> Changes in active site histidine hydrogen bonding trigger cryptochrome activation #MMPMID27551082 Ganguly A; Manahan CC; Top D; Yee EF; Lin C; Young MW; Thiel W; Crane BR Proc Natl Acad Sci U S A 2016[Sep]; 113 (36): 10073-8 PMID27551082show ga There are few detailed mechanistic models that describe how light-sensing proteins convert photochemistry into conformational signals. Combined computational and experimental investigations reveal how photoreduction of the Drosophila cryptochrome (dCRY) flavin induces protonation of a neighboring conserved His residue. Altered His hydrogen bonding then leads to conformational change in a key regulatory element of the protein. These data provide further evidence for involvement of a flavin anionic semiquinone in the dCRY signaling state and allow for the design of variants that can be used to separate dCRY biological functions or as tools for optogenetics. äChanges in active site histidine hydrogen bonding trigger cryptochrome(epmc).pdf DeepDyve Pubget Overpricing