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10.1016/j.bpj.2015.03.038 http://scihub22266oqcxt.onion/10.1016/j.bpj.2015.03.038 C4423040!4423040!25954893     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2015 ; 108 (9): 2362-70 Nephropedia Template TP {{tp|p=25954893|t=2015. Peptide Binding to a PDZ Domain by Electrostatic Steering via Nonnative Salt Bridges |pdf=|usr=}}{{25954893}} gab.com Text Peptide Binding to a PDZ Domain by Electrostatic Steering via Nonnative Salt Bridges JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25954893 #FOAvip We have captured the binding of a peptide to a PDZ domain by unbiased molecular dynamics simulations. Analysis of the trajectories reveals on-pathway encounter complex formation, which is driven by electrostatic interactions between negatively charged carboxylate groups in the peptide and positively charged side chains surrounding the binding site. In contrast, the final stereospecific complex, which matches the crystal structure, features completely different interactions, namely the burial of the hydrophobic side chain of the peptide C-terminal residue and backbone hydrogen bonds. The simulations show that nonnative salt bridges stabilize kinetically the encounter complex during binding. Unbinding follows the inverse sequence of events with the same nonnative salt bridges in the encounter complex. Thus, in contrast to protein folding, which is driven by native interactions, the binding of charged peptides can be steered by nonnative interactions, which might be a general mechanism, e.g., in the recognition of histone tails by bromodomains. Twit Text FOAVip Peptide Binding to a PDZ Domain by Electrostatic Steering via Nonnative Salt Bridges ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25954893 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25954893 #FOAvip English Wikipedia <ref>{{Cite pmid|25954893}}</ref> Peptide Binding to a PDZ Domain by Electrostatic Steering via Nonnative Salt Bridges #MMPMID25954893 Blöchliger N; Xu M; Caflisch A Biophys J 2015[May]; 108 (9): 2362-70 PMID25954893show ga We have captured the binding of a peptide to a PDZ domain by unbiased molecular dynamics simulations. Analysis of the trajectories reveals on-pathway encounter complex formation, which is driven by electrostatic interactions between negatively charged carboxylate groups in the peptide and positively charged side chains surrounding the binding site. In contrast, the final stereospecific complex, which matches the crystal structure, features completely different interactions, namely the burial of the hydrophobic side chain of the peptide C-terminal residue and backbone hydrogen bonds. The simulations show that nonnative salt bridges stabilize kinetically the encounter complex during binding. Unbinding follows the inverse sequence of events with the same nonnative salt bridges in the encounter complex. Thus, in contrast to protein folding, which is driven by native interactions, the binding of charged peptides can be steered by nonnative interactions, which might be a general mechanism, e.g., in the recognition of histone tails by bromodomains. äPeptide Binding to a PDZ Domain by Electrostatic Steering via Nonnativ(epmc).pdf DeepDyve Pubget Overpricing