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Molecular‐modeling calculations of enzymatic enantioselectivity taking hydration into account
Author(s) -
Ke Tao,
Tidor Bruce,
Klibanov Alexander M.
Publication year - 1998
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19980320)57:6<741::aid-bit11>3.0.co;2-a
Subject(s) - molecular mechanics , solvation , molecular dynamics , molecular model , chemistry , computational chemistry , solvent effects , solvent , substrate (aquarium) , organic chemistry , oceanography , geology
A new molecular‐modeling methodology has been applied to explain enzymatic enantioselectivity in water. This methodology, which combines vacuum molecular mechanics and the continuum solvation method, should provide a more realistic view of the solvent–enzyme and solvent–substrate interactions than the heretofore used approaches involving the vacuum molecular mechanics only. The methodology described herein has been validated using the experimental data on α‐chymotrypsin's enantioselectivity in the hydrolysis of four chiral substrates. The reasons why the vacuum molecular mechanics, although not taking hydration into account, still in most cases provide a satisfactory approximation of reality are discussed. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 57: 741–745, 1998