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10.1016/j.cell.2016.09.010 http://scihub22266oqcxt.onion/10.1016/j.cell.2016.09.010 C5451116!5451116 !27662088     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27662088 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell 2016 ; 167 (1 ): 158-170.e12 Nephropedia Template TP {{tp|p=27662088 |t=2016. Structured States of Disordered Proteins from Genomic Sequences |pdf=|usr=}}{{27662088 }} gab.com Text Structured States of Disordered Proteins from Genomic Sequences JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=27662088 #FOAvip Protein flexibility ranges from simple hinge movements to functional disorder. Around half of all human proteins contain apparently disordered regions with little 3D or functional information, and many of these proteins are associated with disease. Building on the evolutionary couplings approach previously successful in predicting 3D states of ordered proteins and RNA, we developed a method to predict the potential for ordered states for all apparently disordered proteins with sufficiently rich evolutionary information. The approach is highly accurate (79%) for residue interactions as tested in more than 60 known disordered regions captured in a bound or specific condition. Assessing the potential for structure of more than 1,000 apparently disordered regions of human proteins reveals a continuum of structural order with at least 50% with clear propensity for three- or two-dimensional states. Co-evolutionary constraints reveal hitherto unseen structures of functional importance in apparently disordered proteins. Twit Text FOAVip Structured States of Disordered Proteins from Genomic Sequences ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=27662088 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27662088 #FOAvip English Wikipedia <ref>{{Cite pmid|27662088 }}</ref> Structured States of Disordered Proteins from Genomic Sequences #MMPMID27662088 Toth-Petroczy A ; Palmedo P ; Ingraham J ; Hopf TA ; Berger B ; Sander C ; Marks DS Cell 2016[Sep]; 167 (1 ): 158-170.e12 PMID27662088 show ga Protein flexibility ranges from simple hinge movements to functional disorder. Around half of all human proteins contain apparently disordered regions with little 3D or functional information, and many of these proteins are associated with disease. Building on the evolutionary couplings approach previously successful in predicting 3D states of ordered proteins and RNA, we developed a method to predict the potential for ordered states for all apparently disordered proteins with sufficiently rich evolutionary information. The approach is highly accurate (79%) for residue interactions as tested in more than 60 known disordered regions captured in a bound or specific condition. Assessing the potential for structure of more than 1,000 apparently disordered regions of human proteins reveals a continuum of structural order with at least 50% with clear propensity for three- or two-dimensional states. Co-evolutionary constraints reveal hitherto unseen structures of functional importance in apparently disordered proteins. |Directed Molecular Evolution/methods [MESH] |Genomics [MESH] |Humans [MESH] |Intrinsically Disordered Proteins/*chemistry/genetics [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH]Structured States of Disordered Proteins from Genomic Sequences (epmc).pdf DeepDyve Pubget Overpricing