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10.1038/nature19791 http://scihub22266oqcxt.onion/10.1038/nature19791 C5161715!5161715!27626386     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nature 2016 ; 538 (7625): 329-35 Nephropedia Template TP {{tp|p=27626386|t=2016. Accurate de novo design of hyperstable constrained peptides |pdf=|usr=}}{{27626386}} gab.com Text Accurate de novo design of hyperstable constrained peptides JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=27626386 #FOAvip Naturally occurring, pharmacologically active peptides constrained with covalent crosslinks generally have shapes evolved to fit precisely into binding pockets on their targets. Such peptides can have excellent pharmaceutical properties, combining the stability and tissue penetration of small molecule drugs with the specificity of much larger protein therapeutics. The ability to design constrained peptides with precisely specified tertiary structures would enable the design of shape-complementary inhibitors of arbitrary targets. Here we describe the development of computational methods for de novo design of conformationally-restricted peptides, and the use of these methods to design 15?50 residue disulfide-crosslinked and heterochiral N-C backbone-cyclized peptides. These peptides are exceptionally stable to thermal and chemical denaturation, and twelve experimentally-determined X-ray and NMR structures are nearly identical to the computational models. The computational design methods and stable scaffolds presented here provide the basis for development of a new generation of peptide-based drugs. Twit Text FOAVip Accurate de novo design of hyperstable constrained peptides ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=27626386 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27626386 #FOAvip English Wikipedia <ref>{{Cite pmid|27626386}}</ref> Accurate de novo design of hyperstable constrained peptides #MMPMID27626386 Bhardwaj G; Mulligan VK; Bahl CD; Gilmore JM; Harvey PJ; Cheneval O; Buchko GW; Pulavarti SV; Kaas Q; Eletsky A; Huang PS; Johnsen WA; Greisen P; Rocklin GJ; Song Y; Linsky TW; Watkins A; Rettie SA; Xu X; Carter LP; Bonneau R; Olson JM; Coutsias E; Correnti CE; Szyperski T; Craik DJ; Baker D Nature 2016[Oct]; 538 (7625): 329-35 PMID27626386show ga Naturally occurring, pharmacologically active peptides constrained with covalent crosslinks generally have shapes evolved to fit precisely into binding pockets on their targets. Such peptides can have excellent pharmaceutical properties, combining the stability and tissue penetration of small molecule drugs with the specificity of much larger protein therapeutics. The ability to design constrained peptides with precisely specified tertiary structures would enable the design of shape-complementary inhibitors of arbitrary targets. Here we describe the development of computational methods for de novo design of conformationally-restricted peptides, and the use of these methods to design 15?50 residue disulfide-crosslinked and heterochiral N-C backbone-cyclized peptides. These peptides are exceptionally stable to thermal and chemical denaturation, and twelve experimentally-determined X-ray and NMR structures are nearly identical to the computational models. The computational design methods and stable scaffolds presented here provide the basis for development of a new generation of peptide-based drugs. äAccurate de novo design of hyperstable constrained peptides (epmc).pdf DeepDyve Pubget Overpricing