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10.1016/j.sbi.2021.05.007 http://scihub22266oqcxt.onion/10.1016/j.sbi.2021.05.007 34214927!ä!34214927 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Curr+Opin+Struct+Biol 2021 ; 71 (ä): 36-42 Nephropedia Template TP {{tp|p=34214927|t=2021. Neutron crystallography for the elucidation of enzyme catalysis |pdf=|usr=}}{{34214927}} gab.com Text Neutron crystallography for the elucidation of enzyme catalysis JO: Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=34214927 #FOAvip Hydrogen atoms and hydration water molecules in proteins are indispensable for many biochemical processes, especially enzymatic catalysis. The locations of hydrogen atoms in proteins are usually predicted based on X-ray structures, but it is still very difficult to know the ionization states of the catalytic residues, the hydration structure of the protein, and the characteristics of hydrogen-bonding interactions. Neutron crystallography allows the direct observation of hydrogen atoms that play crucial roles in molecular recognition and the catalytic reactions of enzymes. In this review, we present the current status of neutron crystallography in structural biology and recent neutron structural analyses of three enzymes: ascorbate peroxidase, the main protease of severe acute respiratory syndrome coronavirus 2, and copper-containing nitrite reductase. Twit Text FOAVip Neutron crystallography for the elucidation of enzyme catalysis ????Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=34214927 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34214927 #FOAvip English Wikipedia <ref>{{Cite pmid|34214927}}</ref> Neutron crystallography for the elucidation of enzyme catalysis #MMPMID34214927 Kono F; Tamada T Curr Opin Struct Biol 2021[Dec]; 71 (ä): 36-42 PMID34214927show ga Hydrogen atoms and hydration water molecules in proteins are indispensable for many biochemical processes, especially enzymatic catalysis. The locations of hydrogen atoms in proteins are usually predicted based on X-ray structures, but it is still very difficult to know the ionization states of the catalytic residues, the hydration structure of the protein, and the characteristics of hydrogen-bonding interactions. Neutron crystallography allows the direct observation of hydrogen atoms that play crucial roles in molecular recognition and the catalytic reactions of enzymes. In this review, we present the current status of neutron crystallography in structural biology and recent neutron structural analyses of three enzymes: ascorbate peroxidase, the main protease of severe acute respiratory syndrome coronavirus 2, and copper-containing nitrite reductase. |*COVID-19[MESH] |*SARS-CoV-2[MESH] |Catalysis[MESH] |Crystallography[MESH] |Crystallography, X-Ray[MESH] |Humans[MESH] |Hydrogen Bonding[MESH] |Models, Molecular[MESH]Neutron crystallography for the elucidation of enzyme catalysis (epmc).pdf DeepDyve Pubget Overpricing