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Cover Picture: Impaired Chaperone Activity of Human Heat Shock Protein Hsp27 Site‐Specifically Modified with Argpyrimidine (Angew. Chem. Int. Ed. 38/2016)
Author(s) -
Matveenko Maria,
Cichero Elena,
Fossa Paola,
Becker Christian F. W.
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201606538
Subject(s) - hsp27 , int , chaperone (clinical) , chemistry , nucleophile , heat shock protein , biophysics , electrophile , arginine , biochemistry , stereochemistry , hsp70 , biology , gene , amino acid , computer science , medicine , pathology , operating system , catalysis
Non‐enzymatic variations of posttranslational modifications (nPTMs) form through reactions of electrophilic metabolites (here, in the eye) with nucleophilic protein side chains (arginine in the hourglass). Such modifications accumulate over time, but are poorly understood at the molecular level. In their Communication on page 11397 ff., C. F. W. Becker and co‐workers report on the impact of the nPTM argpyrimidine on the structure and activity of a human chaperone protein. (Image: iStock.com/Dmytro Kozlov.)