This work is funded by the Natural Science and Engineering Research Council of Canada (NSERC), the Canadian Foundation for Innovation (CFI), and an Ontario Ministry of Research and Innovation (MRI) Early Researcher Award.
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Communication
Conformer Selection and Intensified Dynamics During Catalytic Turnover in Chymotrypsin†
Article first published online: 31 AUG 2012
DOI: 10.1002/anie.201204903
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Issue
Angewandte Chemie International Edition
Volume 51, Issue 38, pages 9666–9669, September 17, 2012
Additional Information
How to Cite
Liuni, P., Jeganathan, A. and Wilson, D. J. (2012), Conformer Selection and Intensified Dynamics During Catalytic Turnover in Chymotrypsin . Angew. Chem. Int. Ed., 51: 9666–9669. doi: 10.1002/anie.201204903
- †
Publication History
- Issue published online: 13 SEP 2012
- Article first published online: 31 AUG 2012
- Manuscript Revised: 31 JUL 2012
- Manuscript Received: 22 JUN 2012
Funded by
- Natural Science and Engineering Research Council of Canada (NSERC)
- Canadian Foundation for Innovation (CFI)
- Ontario Ministry of Research and Innovation (MRI)
Keywords:
- enzymatic catalysis;
- enzyme dynamics;
- H/D exchange;
- mass spectrometry;
- protein dynamics
Intensified searching: In enzymes, conformational dynamics are linked to the catalytic reaction coordinate. A novel analytical approach was used to monitor catalysis-linked dynamics in chymotrypsin, revealing that in some enzymes, catalysis is promoted by intensified, but undirected conformational sampling after substrate binding.