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Designing protein β-sheet surfaces by Z-score optimization

Street, Arthur G. and Datta, Deepshikha and Gordon, D. Benjamin and Mayo, Stephen L. (2000) Designing protein β-sheet surfaces by Z-score optimization. Physical Review Letters, 84 (21). pp. 5010-5013. ISSN 0031-9007. http://resolver.caltech.edu/CaltechAUTHORS:20110620-160435469

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Abstract

Studies of lattice models of proteins have suggested that the appropriate energy expression for protein design may include nonthermodynamic terms to accommodate negative design concerns. One method, developed in lattice model studies, maximizes a quantity known as the "Z-score," which compares the lowest energy sequence whose ground state structure is the target structure to an ensemble of random sequences. Here we show that, in certain circumstances, the technique can be applied to real proteins. The resulting energy expression is used to design the β-sheet surfaces of two real proteins. We find experimentally that the designed proteins are stable and well folded, and in one case is even more thermostable than the wild type.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1103/PhysRevLett.84.5010DOIUNSPECIFIED
http://prl.aps.org/abstract/PRL/v84/i21/p5010_1PublisherUNSPECIFIED
Additional Information:© 2000 American Physical Society. Received 27 September 1999; published in the issue dated 22 May 2000.
Subject Keywords:Protein Structure: Secondary, Proteins, Thermodynamics, Models: Chemical
Classification Code:PACS: 87.15.Aa, 87.10.+e, 87.14.Ee, 87.15.Cc
Record Number:CaltechAUTHORS:20110620-160435469
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20110620-160435469
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:24134
Collection:CaltechAUTHORS
Deposited By: Marie Ary
Deposited On:21 Jun 2011 21:17
Last Modified:26 Dec 2012 13:20

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