Robustness and efficiency in inverse protein folding
Fink, Thomas M. A. and Ball, R. C.. (1997) Robustness and efficiency in inverse protein folding. Physica D: Nonlinear Phenomena, Vol.107 (No.2-4). pp. 199-203. ISSN 0167-2789Full text not available from this repository.
Official URL: http://dx.doi.org/10.1016/S0167-2789(97)00087-0
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|
|Page Range:||pp. 199-203|
|References:|| E.I. Shakhnovich, Phys. Rev. Lett. 72 (1994) 3907.  S. Miyazawa and R. Jernigan, Macromolecules 18 (1985) 534.  W.J.C. Orr, Trans. Faraday Soc. 43 (1947) 12.  Thomas M. Fink and Robin C. Ball, submitted to Phys. Rev. Lett. (1996).|
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