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Cover Feature: A Designed Enzyme Promotes Selective Post‐translational Acylation (ChemBioChem 15/2018)
Author(s) -
Gosavi Pallavi M.,
Jayachandran Megha,
Rempillo Joel J. L.,
Zozulia Oleksii,
Makhlynets Olga V.,
Korendovych Ivan V.
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800365
Subject(s) - cover (algebra) , esterase , acylation , chemistry , feature (linguistics) , calmodulin , computational biology , posttranslational modification , structural biology , molecular recognition , protein engineering , enzyme , biochemistry , stereochemistry , combinatorial chemistry , biology , organic chemistry , mechanical engineering , linguistics , philosophy , engineering , catalysis , molecule
The cover feature picture shows how a computationally designed allosterically regulated esterase CaM M144H, a derivative of AlleyCatE, can recognize and specifically post‐translationally modify helical domains (highlighted in green) in calmodulin‐binding proteins with an unnatural tag providing structural and functional insight into protein–protein interactions. More information can be found in the communication by O. V. Makhlynets, I. V. Korendovych, et al. on page 1605 in Issue 15, 2018 (DOI: 10.1002/cbic.201800196).