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Electrostatics in computational protein design

Vizcarra, Christina L. and Mayo, Stephen L. (2005) Electrostatics in computational protein design. Current Opinion in Chemical Biology, 9 (6). pp. 622-626. ISSN 1367-5931. http://resolver.caltech.edu/CaltechAUTHORS:20110620-160432503

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Abstract

Catalytic activity and protein-protein recognition have proven to be significant challenges for computational protein design. Electrostatic interactions are crucial for these and other protein functions, and therefore accurate modeling of electrostatics is necessary for successfully advancing protein design into the realm of protein function. This review focuses on recent progress in modeling electrostatic interactions in computational protein design, with particular emphasis on continuum models.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/j.cbpa.2005.10.014 DOIUNSPECIFIED
http://www.sciencedirect.com/science/article/pii/S1367593105001444PublisherUNSPECIFIED
Additional Information:© 2005 Elsevier Ltd. Available online 28 October 2005. This work was funded by Howard Hughes Medical Institute, the Ralph M Parsons Foundation, the Defense Advanced Research Projects Agency, the Institute for Collaborative Biotechnologies (grant DAAD19-03-D-0004 from the US Army Research Office) (SLM), and the National Science Foundation (CLV). We wish to thank Benjamin D Allen for comments on the manuscript.
Funders:
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Ralph M. Parsons FoundationUNSPECIFIED
Defense Advanced Research Projects Agency (DARPA)DAAD19-03-D-0004
NSFUNSPECIFIED
Subject Keywords:Computer Simulation; Models: Theoretical; Protein Conformation; Proteins; Static Electricity
Record Number:CaltechAUTHORS:20110620-160432503
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20110620-160432503
Official Citation:Christina L Vizcarra, Stephen L Mayo, Electrostatics in computational protein design, Current Opinion in Chemical Biology, Volume 9, Issue 6, December 2005, Pages 622-626, ISSN 1367-5931, 10.1016/j.cbpa.2005.10.014.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:24116
Collection:CaltechAUTHORS
Deposited By: Marie Ary
Deposited On:27 Sep 2011 20:17
Last Modified:27 Sep 2011 20:17

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