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Cover Image, Volume 35, Issue 19
Publication year - 2014
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.23663
Subject(s) - cover (algebra) , citation , volume (thermodynamics) , computer science , chemistry , dihydrofolate reductase , information retrieval , enzyme , combinatorics , world wide web , physics , biochemistry , mathematics , thermodynamics , engineering , mechanical engineering
Recent studies have proposed that enzymes involve networks of coupled residues throughout the protein that participate in motions accompanying the chemical barrier crossing. On page 1411 (DOI: 10.1002/jcc.23629 ), Daniel Roston et al. use QM/MM simulations to reproduce experimental rates for the wild type and distal mutants of Escherichia coli dihydrofolate reductase, and detail how residues remote from the active site affect the catalyzed chemistry. The distance matrix on the cover shows changes in the distance between α‐carbons of each enzyme in going from the reactant to the transition states.