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Simple electrostatic model improves designed protein sequences

Zollars, Eric S. and Marshall, Shannon A. and Mayo, Stephen L. (2006) Simple electrostatic model improves designed protein sequences. Protein Science, 15 (8). pp. 2014-2018. ISSN 0961-8368. http://resolver.caltech.edu/CaltechAUTHORS:20110620-160436627

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Abstract

Electrostatic interactions are important for both protein stability and function, including binding and catalysis. As protein design moves into these areas, an accurate description of electrostatic energy becomes necessary. Here, we show that a simple distance-dependent Coulombic function parameterized by a comparison to Poisson-Boltzmann calculations is able to capture some of these electrostatic interactions. Specifically, all three helix N-capping interactions in the engrailed homeodomain fold are recovered using the newly parameterized model. The stability of this designed protein is similar to a protein forced by sequence restriction to have beneficial electrostatic interactions.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1110/ps.062105506DOIUNSPECIFIED
http://onlinelibrary.wiley.com/doi/10.1110/ps.062105506/abstractPublisherUNSPECIFIED
Contact Email Address:steve@mayo.caltech.edu
Additional Information:© 2006 The Protein Society. Published by Cold Spring Harbor Laboratory Press. Received January 24, 2006; Final Revision May 12, 2006; Accepted May 15, 2006. Article first published online: 1 Jan. 2009. This work was supported by the Howard Hughes Medical Institute and the Ralph M. Parsons Foundation. E.S.Z. would like to thank the ARCS Foundation for funding.
Funders:
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Ralph M. Parsons FoundationUNSPECIFIED
ARCS FoundationUNSPECIFIED
Subject Keywords:Protein Denaturation, Protein Engineering, Homeodomain Proteins, Animals, Static Electricity, Sequence Alignment, Molecular Sequence Data, Models: Molecular, Protein Structure: Secondary, Amino Acid Sequence, Transcription Factors
Non-Subject Keywords:protein design, electrostatics, engrailed, N-capping
Record Number:CaltechAUTHORS:20110620-160436627
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20110620-160436627
Official Citation:Zollars, E. S., Marshall, S. A. and Mayo, S. L. (2006), Simple electrostatic model improves designed protein sequences. Protein Science, 15: 2014–2018. doi: 10.1110/ps.062105506
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:24141
Collection:CaltechAUTHORS
Deposited By: Marie Ary
Deposited On:21 Jun 2011 14:40
Last Modified:23 Aug 2016 10:02

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