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


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

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1C9O 1999-08-03T00:00:00+0000 1.17 CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP
1HZ9 2001-01-24T00:00:00+0000 1.8 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
1HZA 2001-01-24T00:00:00+0000 1.8 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
1HZB 2001-01-24T00:00:00+0000 1.28 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
1HZC 2001-01-24T00:00:00+0000 1.32 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
1I5F 2001-02-27T00:00:00+0000 1.4 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
2HAX 2006-06-13T00:00:00+0000 1.29 Crystal structure of Bacillus caldolyticus cold shock protein in complex with hexathymidine
5JX4 2016-05-12T00:00:00+0000 1.8 Crystal structure of E36-G37del mutant of the Bacillus caldolyticus cold shock protein.
1CSP 1993-05-12T00:00:00+0000 2.45 CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN
1CSQ 1993-05-12T00:00:00+0000 2.7 CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN

Relevant UniProtKB Entries

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