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Dynamics of Ordered Water in Interfacial Enzyme Recognition: Bovine Pancreatic Phospholipase A2

Zhao, Liang and Pal, Samir Kumar and Xia, Tianbing and Zewail, Ahmed H. (2004) Dynamics of Ordered Water in Interfacial Enzyme Recognition: Bovine Pancreatic Phospholipase A2. Angewandte Chemie International Edition, 43 (1). pp. 60-63. ISSN 1433-7851. doi:10.1002/anie.200352961. https://resolver.caltech.edu/CaltechAUTHORS:20160817-132621558

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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.


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http://dx.doi.org/10.1002/anie.200352961DOIArticle
http://onlinelibrary.wiley.com/doi/10.1002/anie.200352961/abstractPublisherArticle
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.
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Funding AgencyGrant Number
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Subject Keywords:enzymes; femtochemistry; hydration dynamics; lipases; surfactants
Issue or Number:1
DOI:10.1002/anie.200352961
Record Number:CaltechAUTHORS:20160817-132621558
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160817-132621558
Official Citation:Zhao, L., Pal, S. K., Xia, T. and Zewail, A. H. (2004), Dynamics of Ordered Water in Interfacial Enzyme Recognition: Bovine Pancreatic Phospholipase A2. Angew. Chem. Int. Ed., 43: 60–63. doi: 10.1002/anie.200352961
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:69713
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:17 Aug 2016 21:43
Last Modified:11 Nov 2021 04:18

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