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Back Cover: In silico Optimization of a Fragment‐Based Hit Yields Biologically Active, High‐Efficiency Inhibitors for Glutamate Racemase (ChemMedChem 10/2013)
Author(s) -
Whalen Katie L.,
Chau Anthony C.,
Spies M. Ashley
Publication year - 2013
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201390044
Subject(s) - in silico , bacillus subtilis , chemistry , docking (animal) , active site , computational biology , cover (algebra) , molecular dynamics , combinatorial chemistry , biochemistry , enzyme , biology , computational chemistry , bacteria , genetics , medicine , mechanical engineering , nursing , engineering , gene
The back cover picture shows the molecular structure of glutamate racemase from Bacillus subtilis (ribbon) with a novel inhibitor (space‐filling) bound to the active site cleft. The inhibitor was discovered via an in silico lead optimization technique, termed FERM‐SMD, that combines steered molecular dynamics simulations and ensemble docking. For more details, see the Full Paper by M. Ashley Spies et al. on p. 1681 ff.