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10.1038/srep36895 http://scihub22266oqcxt.onion/10.1038/srep36895 C5118788!5118788 !27874096     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27874096 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2016 ; 6 (ä): 36895 Nephropedia Template TP {{tp|p=27874096 |t=2016. Complex lasso: new entangled motifs in proteins |pdf=|usr=}}{{27874096 }} gab.com Text Complex lasso: new entangled motifs in proteins JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27874096 #FOAvip We identify new entangled motifs in proteins that we call complex lassos. Lassos arise in proteins with disulfide bridges (or in proteins with amide linkages), when termini of a protein backbone pierce through an auxiliary surface of minimal area, spanned on a covalent loop. We find that as much as 18% of all proteins with disulfide bridges in a non-redundant subset of PDB form complex lassos, and classify them into six distinct geometric classes, one of which resembles supercoiling known from DNA. Based on biological classification of proteins we find that lassos are much more common in viruses, plants and fungi than in other kingdoms of life. We also discuss how changes in the oxidation/reduction potential may affect the function of proteins with lassos. Lassos and associated surfaces of minimal area provide new, interesting and possessing many potential applications geometric characteristics not only of proteins, but also of other biomolecules. Twit Text FOAVip Complex lasso: new entangled motifs in proteins ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=27874096 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27874096 #FOAvip English Wikipedia <ref>{{Cite pmid|27874096 }}</ref> Complex lasso: new entangled motifs in proteins #MMPMID27874096 Niemyska W ; Dabrowski-Tumanski P ; Kadlof M ; Haglund E ; Su?kowski P ; Sulkowska JI Sci Rep 2016[Nov]; 6 (ä): 36895 PMID27874096 show ga We identify new entangled motifs in proteins that we call complex lassos. Lassos arise in proteins with disulfide bridges (or in proteins with amide linkages), when termini of a protein backbone pierce through an auxiliary surface of minimal area, spanned on a covalent loop. We find that as much as 18% of all proteins with disulfide bridges in a non-redundant subset of PDB form complex lassos, and classify them into six distinct geometric classes, one of which resembles supercoiling known from DNA. Based on biological classification of proteins we find that lassos are much more common in viruses, plants and fungi than in other kingdoms of life. We also discuss how changes in the oxidation/reduction potential may affect the function of proteins with lassos. Lassos and associated surfaces of minimal area provide new, interesting and possessing many potential applications geometric characteristics not only of proteins, but also of other biomolecules. |Animals [MESH] |Databases, Protein [MESH] |Disulfides/chemistry [MESH] |Fungi/metabolism [MESH] |Oxidoreductases/chemistry/metabolism [MESH] |Plants/metabolism [MESH] |Protein Structure, Secondary [MESH]Complex lasso: new entangled motifs in proteins (epmc).pdf DeepDyve Pubget Overpricing