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10.1073/pnas.1414188111 http://scihub22266oqcxt.onion/10.1073/pnas.1414188111 C4273357!4273357!25468976     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (50): 17732-6 Nephropedia Template TP {{tp|p=25468976|t=2014. Observation of ice-like water layers at an aqueous protein surface |pdf=|usr=}}{{25468976}} gab.com Text Observation of ice-like water layers at an aqueous protein surface JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25468976 #FOAvip Antifreeze proteins (AFPs) enable the survival of various organisms in freezing or subfreezing habitats by preventing the macroscopic growth of ice crystals. Understanding how AFPs recognize and bind ice crystals is the most important step to unravel their working mechanism. Using surface-specific sum frequency generation spectroscopy, we were able to directly probe the ice-binding site of the protein and discovered that, already at room temperature and in an aqueous solution, the antifreeze proteins arrange water molecules into an ice-like array, which they then use to bind to ice crystals. Twit Text FOAVip Observation of ice-like water layers at an aqueous protein surface ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25468976 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25468976 #FOAvip English Wikipedia <ref>{{Cite pmid|25468976}}</ref> Observation of ice-like water layers at an aqueous protein surface #MMPMID25468976 Meister K; Strazdaite S; DeVries AL; Lotze S; Olijve LLC; Voets IK; Bakker HJ Proc Natl Acad Sci U S A 2014[Dec]; 111 (50): 17732-6 PMID25468976show ga Antifreeze proteins (AFPs) enable the survival of various organisms in freezing or subfreezing habitats by preventing the macroscopic growth of ice crystals. Understanding how AFPs recognize and bind ice crystals is the most important step to unravel their working mechanism. Using surface-specific sum frequency generation spectroscopy, we were able to directly probe the ice-binding site of the protein and discovered that, already at room temperature and in an aqueous solution, the antifreeze proteins arrange water molecules into an ice-like array, which they then use to bind to ice crystals. äObservation of ice-like water layers at an aqueous protein surface (epmc).pdf DeepDyve Pubget Overpricing