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10.1002/anie.201705512 http://scihub22266oqcxt.onion/10.1002/anie.201705512 C5575531!5575531!28613440     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Angew+Chem+Int+Ed+Engl 2017 ; 56 (31): 9151-4 Nephropedia Template TP {{tp|p=28613440|t=2017. The Existence of an Isolated Hydronium Ion in the Interior of Proteins |pdf=|usr=}}{{28613440}} gab.com Text The Existence of an Isolated Hydronium Ion in the Interior of Proteins JO: Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=28613440 #FOAvip Neutron diffraction analysis studies reported an isolated hydronium ion (H3O+) in the interior of d?xylose isomerase (XI) and phycocyanobilin?ferredoxin oxidoreductase (PcyA). H3O+ forms hydrogen bonds (H?bonds) with two histidine side?chains and a backbone carbonyl group in PcyA, whereas H3O+ forms H?bonds with three acidic residues in XI. Using a quantum mechanical/molecular mechanical (QM/MM) approach, we analyzed stabilization of H3O+ by the protein environment. QM/MM calculations indicated that H3O+ was unstable in the PcyA crystal structure, releasing a proton to an H?bond partner His88, producing H2O and protonated His88. On the other hand, H3O+ was stable in the XI crystal structure. H?bond partners of isolated H3O+ would be practically limited to acidic residues such as aspartic and glutamic acids in the protein environment. Twit Text FOAVip The Existence of an Isolated Hydronium Ion in the Interior of Proteins ????Angew Chem Int Ed Engl http://www.kidney.de/pget.php?&tw=1&pmid=28613440 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28613440 #FOAvip English Wikipedia <ref>{{Cite pmid|28613440}}</ref> The Existence of an Isolated Hydronium Ion in the Interior of Proteins #MMPMID28613440 Ikeda T; Saito K; Hasegawa R; Ishikita H Angew Chem Int Ed Engl 2017[Jul]; 56 (31): 9151-4 PMID28613440show ga Neutron diffraction analysis studies reported an isolated hydronium ion (H3O+) in the interior of d?xylose isomerase (XI) and phycocyanobilin?ferredoxin oxidoreductase (PcyA). H3O+ forms hydrogen bonds (H?bonds) with two histidine side?chains and a backbone carbonyl group in PcyA, whereas H3O+ forms H?bonds with three acidic residues in XI. Using a quantum mechanical/molecular mechanical (QM/MM) approach, we analyzed stabilization of H3O+ by the protein environment. QM/MM calculations indicated that H3O+ was unstable in the PcyA crystal structure, releasing a proton to an H?bond partner His88, producing H2O and protonated His88. On the other hand, H3O+ was stable in the XI crystal structure. H?bond partners of isolated H3O+ would be practically limited to acidic residues such as aspartic and glutamic acids in the protein environment. äThe Existence of an Isolated Hydronium Ion in the Interior of Proteins(epmc).pdf DeepDyve Pubget Overpricing