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
ID: E9QTsXHm
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:53 p.m.
Version: 1
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Percent Identity | Matching Chains | Protein | Accession | Entry Name |
---|---|---|---|---|
100.0 | Cold shock protein CspB | P41016 | CSPB_BACCL | |
98.5 | Cold shock protein CspB | P42016 | CSPB_GEOSE | |
100.0 | Cold shock protein CspB | P32081 | CSPB_BACSU | |
92.3 | Cold shock protein CspB | Q81K90 | CSPD_BACAN | |
92.3 | Cold shock protein CspB | Q816H3 | CSPD_BACCR | |
96.5 | Cold shock protein CspB | P41018 | CSPB_SPOGL |