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Cover Picture: Monitoring Conformational Changes in the NDM‐1 Metallo‐β‐lactamase by 19 F NMR Spectroscopy (Angew. Chem. Int. Ed. 12/2014)
Author(s) -
Rydzik Anna M.,
Brem Jürgen,
van Berkel Sander S.,
Pfeffer Inga,
Makena Anne,
Claridge Timothy D. W.,
Schofield Christopher J.
Publication year - 2014
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.201401104
Subject(s) - nuclear magnetic resonance spectroscopy , chemistry , spectroscopy , active site , chemical shift , stereochemistry , crystallography , organic chemistry , enzyme , physics , quantum mechanics
Increasing antibiotic resistance is a global health concern. Metallo‐β‐lactamases catalyze the hydrolysis of almost all β‐lactam antibiotics. T. D. W. Claridge, C. J. Schofield et al. show in their Communication on page 3129 ff. how 19 F NMR spectroscopy can be used to investigate the binding mode of inhibitors to the New Delhi Metallo‐β‐lactamase I (NDM‐1). By labeling an active‐site loop with 19 F, changes in the local chemical environment caused by inhibitor binding can be readily monitored by NMR spectroscopy.