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Robustness and efficiency in inverse protein folding

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Fink, Thomas M. A. and Ball, Robin (1997) Robustness and efficiency in inverse protein folding. Physica D: Nonlinear Phenomena, Vol.107 (No.2-4). pp. 199-203. doi:10.1016/S0167-2789(97)00087-0

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Official URL: http://dx.doi.org/10.1016/S0167-2789(97)00087-0

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Abstract

Successful protein design is characterized by two criteria: thermodynamic robustness, the probability of occupation of the target conformation, and kinetic efficiency, the ability of the protein to quickly fold to its target state. We observe a conflict between robustness and efficiency upon variation of both the pair potential matrix and the designed sequence. We argue that marginal reduction in thermodynamic robustness can provide significant increase in kinetic efficiency, thereby allowing improved protein design.

Item Type: Journal Article
Subjects: Q Science > QC Physics
Q Science > QP Physiology
T Technology > TP Chemical technology
Divisions: Faculty of Science > Physics
Library of Congress Subject Headings (LCSH): Protein folding, Protein engineering
Journal or Publication Title: Physica D: Nonlinear Phenomena
Publisher: Elsevier BV
ISSN: 0167-2789
Official Date: 1997
Dates:
DateEvent
1997Published
Volume: Vol.107
Number: No.2-4
Page Range: pp. 199-203
DOI: 10.1016/S0167-2789(97)00087-0
Status: Peer Reviewed
Publication Status: Published

Data sourced from Thomson Reuters' Web of Knowledge

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