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PEDS Advance Access published online on May 23, 2006
Protein Engineering Design and Selection, doi:10.1093/protein/gzl019
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© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received March 13, 2006
Revised April 7, 2006
Accepted April 12, 2006

Article

The correlation between protein stability and dipole moment: a critical test

Michael Wunderlich 1 and Franz X. Schmid 1 *

1 Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, D-95440 Bayreuth, Germany

* To whom correspondence should be addressed.
Franz X. Schmid, E-mail: fx.schmid{at}uni-bayreuth.de


  Abstract

Improving the stability of proteins is a major aim in basic and applied protein science. Querol and coworkers calculated changes in the quasi-electric dipole moment of a protein and used it as a simple criterion to predict stabilizing charge mutations. They employed this method to propose for the bacterial cold shock protein Bc-Csp a number of charge mutations that should have a strong influence on stability. We produced eight variants of Bc-Csp with such mutations and measured their stabilities experimentally. However, we could not find a correlation between the stability and the quasi dipole moment of these variants. Possibly, the quasi dipole moment reflects only a secondary aspect of the changes that are caused by charge mutations in a protein.

Keywords: cold shock protein; electric dipole moment; electrostatic interactions; protein stabilization.
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