Angewandte Chemie International Edition

Cover image for Vol. 53 Issue 34

Editor: Peter Gölitz, Deputy Editors: Neville Compton, Haymo Ross

Online ISSN: 1521-3773

Associated Title(s): Angewandte Chemie, Chemistry - A European Journal, Chemistry – An Asian Journal, Zeitschrift für Chemie

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Abstracts now required for Communications

To improve the discoverability of Communications, we ask authors to supply an abstract as the first paragraph from now on. In this abstract, the motivation for the work, the methods applied, the results, and the conclusions drawn should be presented (maximum 1000 characters).


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Sergey Troyanov

“My worst nightmare is to have to stop promising scientific work. The most exciting thing about my research is a lot of wonderful (chemical) surprises ...” This and more about Sergey Troyanov can be found on page 8816.

Angew. Chem. Int. Ed.2014, 53, No. 34, 8816

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August 19, 2014

Max Planck Institute for Coal Research Celebrates 100th Anniversary

The Max-Planck-Institut für Kohlenforschung celebrates 100 years of excellence in catalysis research. The Institute opened in 1914 in Mülheim an der Ruhr, Germany. Catalytic processes that are used worldwide have been developed there; a special issue of Angewandte Chemie now showcases the Institute’s history and current topics.

Browse issue 33/2014 now.

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A Larger Pocket

Reprogramed nonribosomal peptide synthetase incorporates amino acids with reactive sites for “click” chemistry

A Larger Pocket - Reprogramed nonribosomal peptide synthetase incorporates amino acids with reactive sites for “click” chemistry

A single targeted mutation is enough to alter a natural peptide system so that it also incorporates non-natural amino acids into peptides, report Swiss scientists in the journal Angewandte Chemie. The mutation increases the size of the binding cavity in one domain of the system, which changes the substrate specificity. The researchers are thus able to incorporate amino acids with a specific reactive group that can later be used to easily modify the peptide.

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