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10.1073/pnas.1422272112 http://scihub22266oqcxt.onion/10.1073/pnas.1422272112 C4311821!4311821!25561557     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       Proc+Natl+Acad+Sci+U+S+A 2015 ; 112 (3): 737-42 Nephropedia Template TP {{tp|p=25561557|t=2015. Flies expand the repertoire of protein structures that bind ice |pdf=|usr=}}{{25561557}} gab.com Text Flies expand the repertoire of protein structures that bind ice JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25561557 #FOAvip A previously unidentified insect antifreeze protein has been characterized in a fly. It is present in the adult stage of midges that emerge from fresh water in the spring and need protection from occasional night frosts. The mature protein has 79 residues and is small and repetitive enough to be reliably modeled as a tightly wound solenoid structure. Each tandem repeat of 10 residues forms a coil of the solenoid that is cross-braced by a disulfide bond. This fold orients a row of seven stacked tyrosine side chains to make a flat surface, which is the predicted ice-binding site of the protein. This protein has no homologs in the database and has, therefore, recently evolved to protect its host from freezing. Twit Text FOAVip Flies expand the repertoire of protein structures that bind ice ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25561557 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25561557 #FOAvip English Wikipedia <ref>{{Cite pmid|25561557}}</ref> Flies expand the repertoire of protein structures that bind ice #MMPMID25561557 Basu K; Graham LA; Campbell RL; Davies PL Proc Natl Acad Sci U S A 2015[Jan]; 112 (3): 737-42 PMID25561557show ga A previously unidentified insect antifreeze protein has been characterized in a fly. It is present in the adult stage of midges that emerge from fresh water in the spring and need protection from occasional night frosts. The mature protein has 79 residues and is small and repetitive enough to be reliably modeled as a tightly wound solenoid structure. Each tandem repeat of 10 residues forms a coil of the solenoid that is cross-braced by a disulfide bond. This fold orients a row of seven stacked tyrosine side chains to make a flat surface, which is the predicted ice-binding site of the protein. This protein has no homologs in the database and has, therefore, recently evolved to protect its host from freezing. äFlies expand the repertoire of protein structures that bind ice (epmc).pdf DeepDyve Pubget Overpricing