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Front Cover: Cryo‐kinetics Reveal Dynamic Effects on the Chemistry of Human Dihydrofolate Reductase (ChemBioChem 14/2021)
Author(s) -
Adesina Aduragbemi S.,
Luk Louis Y. P.,
Allemann Rudolf K.
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202100238
Subject(s) - dihydrofolate reductase , chemistry , front cover , enzyme kinetics , kinetics , isotopologue , enzyme , cover (algebra) , enzyme catalysis , computational chemistry , stereochemistry , biophysics , biochemistry , active site , biology , physics , organic chemistry , molecule , mechanical engineering , quantum mechanics , engineering
Isotopologues, enzymes that differ only in their isotopic substitution, engage in a tug of war to determine the role of protein motions and electrostatics for catalysis. The features of the ribbon diagrams indicate that the enzymes are human dihydrofolate reductases. More information can be found in the Communication by R. K. Allemann et al.