Published December 22, 2004
| public
Journal Article
Dynamics of Ordered Water in Interfacial Enzyme Recognition: Bovine Pancreatic Phospholipase A2
Abstract
Slippery when wet: Water molecules at the interface between a protein (e.g. bovine pancreatic phospholipase A2) and a micellar substrate act as a lubricant and facilitate movement and binding of the protein at the surface (see picture). Studies of the hydration dynamics before and after complexation reveal that these interactions are crucial for enzymatic function.
Additional Information
© 2004 Wiley-VCH Verlag GmbH & Co. Received: September 26, 2003. Published Online: December 8 Dec 2003. Financial support from the National Science Foundation is acknowledged.Additional details
- Eprint ID
- 69713
- DOI
- 10.1002/anie.200352961
- Resolver ID
- CaltechAUTHORS:20160817-132621558
- NSF
- Created
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2016-08-17Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field