Butyrylcholinesterase and G116H, G116S, G117H, G117N, E197Q and G117H/E197Q mutants: A molecular dynamics study

Chemico-Biological Interactions

Volumn 187, Issue 1-3, 2010, Pages 241-245

  Vyas, Shubham ^a   Beck, Jeremy M ^a   Xia, Shijing ^a   Zhang, Jun ^b   Hadad, Christopher M ^a  

^a OHIO STATE UNIVERSITY   (United States)

^b HUMAN BIOMOLECULAR RESEARCH INSTITUTE   (United States)

Author keywords

Butyrylcholinesterase; E197Q; G117H; Molecular dynamics simulations; Organophosphorus nerve agents

Indexed keywords

CHOLINESTERASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MUTATIONAL ANALYSIS; SIMULATION; STOICHIOMETRY; STRUCTURE ANALYSIS; WILD TYPE;

EID: 77955515433     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.04.004     Document Type: Article

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29. Interestingly, W82 slips into the active site in all of the trajectories from its original position; the origin (or ramification) of this effect is not obvious. Such movement of W82 was sometimes noted for other mutants, but was not present in all of the trajectories.