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10.1038/nchembio.2206 http://scihub22266oqcxt.onion/10.1038/nchembio.2206 C5110370!5110370!27748749     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       Nat+Chem+Biol 2016 ; 12 (12): 1084-8 Nephropedia Template TP {{tp|p=27748749|t=2016. A prevalent intraresidue hydrogen bond stabilizes proteins |pdf=|usr=}}{{27748749}} gab.com Text A prevalent intraresidue hydrogen bond stabilizes proteins JO: Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=27748749 #FOAvip Current limitations in de novo protein structure prediction and design suggest an incomplete understanding of the interactions that govern protein folding. Here we demonstrate that previously unappreciated hydrogen bonds occur within proteins between the amide proton and carbonyl oxygen of the same residue. Quantum calculations, infrared spectroscopy, and nuclear magnetic resonance spectroscopy show that these interactions share hallmark features of canonical hydrogen bonds. Biophysical analyses demonstrate that selective attenuation or enhancement of these C5 hydrogen bonds affects the stability of synthetic ?-sheets. These interactions are common, affecting approximately 5% of all residues and 94% of proteins, and their cumulative impact provides several kcal/mol of conformational stability to a typical protein. C5 hydrogen bonds stabilize, especially, the flat ?-sheets of the amyloid state, which is linked with Alzheimer?s disease and other neurodegenerative disorders. Inclusion of these interactions in computational force fields would improve models of protein folding, function, and dysfunction. Twit Text FOAVip A prevalent intraresidue hydrogen bond stabilizes proteins ????Nat Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=27748749 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27748749 #FOAvip English Wikipedia <ref>{{Cite pmid|27748749}}</ref> A prevalent intraresidue hydrogen bond stabilizes proteins #MMPMID27748749 Newberry RW; Raines RT Nat Chem Biol 2016[Dec]; 12 (12): 1084-8 PMID27748749show ga Current limitations in de novo protein structure prediction and design suggest an incomplete understanding of the interactions that govern protein folding. Here we demonstrate that previously unappreciated hydrogen bonds occur within proteins between the amide proton and carbonyl oxygen of the same residue. Quantum calculations, infrared spectroscopy, and nuclear magnetic resonance spectroscopy show that these interactions share hallmark features of canonical hydrogen bonds. Biophysical analyses demonstrate that selective attenuation or enhancement of these C5 hydrogen bonds affects the stability of synthetic ?-sheets. These interactions are common, affecting approximately 5% of all residues and 94% of proteins, and their cumulative impact provides several kcal/mol of conformational stability to a typical protein. C5 hydrogen bonds stabilize, especially, the flat ?-sheets of the amyloid state, which is linked with Alzheimer?s disease and other neurodegenerative disorders. Inclusion of these interactions in computational force fields would improve models of protein folding, function, and dysfunction. äA prevalent intraresidue hydrogen bond stabilizes proteins (epmc).pdf DeepDyve Pubget Overpricing