Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1126/science.aan5774 http://scihub22266oqcxt.onion/10.1126/science.aan5774 C5959285!5959285!29026044     free     free     free Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 225.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2017 ; 358 (6360): 238-41 Nephropedia Template TP {{tp|p=29026044|t=2017. Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water |pdf=|usr=}}{{29026044}} gab.com Text Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=29026044 #FOAvip A substantial fraction of the proteome is intrinsically disordered, and even well-folded proteins adopt non-native geometries during synthesis, folding, transport, and turnover. Characterization of intrinsically disordered proteins (IDPs) is challenging, in part because of a lack of accurate physical models and the difficulty of interpreting experimental results. We have developed a general method to extract the dimensions and solvent quality (self-interactions) of IDPs from a single small-angle x-ray scattering measurement. We applied this procedure to a variety of IDPs and found that even IDPs with low net charge and high hydrophobicity remain highly expanded in water, contrary to the general expectation that protein-like sequences collapse in water. Our results suggest that the unfolded state of most foldable sequences is expanded; we conjecture that this property was selected by evolution to minimize misfolding and aggregation. Twit Text FOAVip Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water ????Science http://www.kidney.de/pget.php?&tw=1&pmid=29026044 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29026044 #FOAvip English Wikipedia <ref>{{Cite pmid|29026044}}</ref> Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water #MMPMID29026044 Riback JA; Bowman MA; Zmyslowski AM; Knoverek CR; Jumper JM; Hinshaw JR; Kaye EB; Freed KF; Clark PL; Sosnick TR Science 2017[Oct]; 358 (6360): 238-41 PMID29026044show ga A substantial fraction of the proteome is intrinsically disordered, and even well-folded proteins adopt non-native geometries during synthesis, folding, transport, and turnover. Characterization of intrinsically disordered proteins (IDPs) is challenging, in part because of a lack of accurate physical models and the difficulty of interpreting experimental results. We have developed a general method to extract the dimensions and solvent quality (self-interactions) of IDPs from a single small-angle x-ray scattering measurement. We applied this procedure to a variety of IDPs and found that even IDPs with low net charge and high hydrophobicity remain highly expanded in water, contrary to the general expectation that protein-like sequences collapse in water. Our results suggest that the unfolded state of most foldable sequences is expanded; we conjecture that this property was selected by evolution to minimize misfolding and aggregation. äInnovative scattering analysis shows that hydrophobic disordered prote(epmc).pdf DeepDyve Pubget Overpricing