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. Study holds ProTherm entries: 22233, 22234, 22235, 22236, 22237, 22238, 22239, 22240, 22241, 22242, 22243, 22244, 22245, 22246, 22247, 22248, 22249, 22250, 22251, 22252, 22253, 22254, 22255, 22256, 22257, 22258, 22259, 22260, 22261, 22262, 22263, 22264, 22265, 22266, 22267, 22268, 22269, 22270 Extra Details: cold shock protein; electric dipole moment; electrostatic interactions; protein stabilization

Submission Details

ID: E9QTsXHm

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:53 p.m.

Version: 1

Publication Details

Wunderlich M;Schmid FX,Protein Eng. Des. Sel. (2006) The correlation between protein stability and dipole moment: a critical test. PMID:16720692

Additional Information