The Library

Robustness and efficiency in inverse protein folding

Tools

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. ISSN 0167-2789

Full text not available from this repository.

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

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:

Date	Event
1997	Published

Volume:

Vol.107

Number:

No.2-4

Page Range:

pp. 199-203

Identification Number:

10.1016/S0167-2789(97)00087-0

Status:

Peer Reviewed

Publication Status:

Published

References:

[1] E.I. Shakhnovich, Phys. Rev. Lett. 72 (1994) 3907.
[2] S. Miyazawa and R. Jernigan, Macromolecules 18 (1985)
534.
[3] W.J.C. Orr, Trans. Faraday Soc. 43 (1947) 12.
[4] Thomas M. Fink and Robin C. Ball, submitted to Phys.
Rev. Lett. (1996).

URI:

http://wrap.warwick.ac.uk/id/eprint/39709

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record