Cover Picture: Impaired Chaperone Activity of Human Heat Shock Protein Hsp27 Site-Specifically Modified with Argpyrimidine (Angew. Chem. Int. Ed. 38/2016)

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• 作者：Dr. Maria Matveenko ; Dr. Elena Cichero ; Prof. Dr. Paola Fossa and Prof. Dr. Christian F. W. Becker
• 刊名：Angewandte Chemie International Edition
• 出版年：2016
• 出版时间：September 12, 2016
• 年：2016
• 卷：55
• 期：38
• 页码：11303
• 全文大小：973K
• ISSN：1521-3773

文摘

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 g/10.1002/anie.201605366" rel="references:http://dx.doi.org/10.1002/anie.201605366">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.)