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
1NMF 1996-07-11 MAJOR COLD-SHOCK PROTEIN, NMR, 20 STRUCTURES
2F52 2006-09-19 Solution structure of cold shock protein CspB from Bacillus subtilis in complex with heptathymidine
1NMG 1996-07-11 MAJOR COLD-SHOCK PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE
1C9O 2000-04-02 1.17 CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS COLD SHOCK PROTEIN BC-CSP
1HZB 2001-11-07 1.28 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
2HAX 2007-04-24 1.29 Crystal structure of Bacillus caldolyticus cold shock protein in complex with hexathymidine
1HZC 2001-11-07 1.32 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
3PF4 2011-09-21 1.38 Crystal structure of Bs-CspB in complex with r(GUCUUUA)
1I5F 2001-11-07 1.4 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
3PF5 2011-09-21 1.68 Crystal structure of Bs-CspB in complex with rU6
2ES2 2006-09-05 1.78 Crystal Structure Analysis of the Bacillus Subtilis Cold Shock Protein Bs-CspB in Complex with Hexathymidine
1HZ9 2001-11-07 1.8 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
1HZA 2001-11-07 1.8 BACILLUS CALDOLYTICUS COLD-SHOCK PROTEIN MUTANTS TO STUDY DETERMINANTS OF PROTEIN STABILITY
5JX4 2017-05-10 1.8 Crystal structure of E36-G37del mutant of the Bacillus caldolyticus cold shock protein.
2I5M 2007-05-22 2.3 Crystal structure of Bacillus subtilis cold shock protein CspB variant A46K S48R
1CSP 1995-05-12 2.45 CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN
2I5L 2007-05-22 2.55 Crystal structure of Bacillus subtilis Cold Shock Protein variant Bs-CspB M1R/E3K/K65I
1CSQ 1995-05-12 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
98.5 Cold shock protein CspB P42016 CSPB_GEOSE
100.0 Cold shock protein CspB P41016 CSPB_BACCL
96.5 Cold shock protein CspB P41018 CSPB_SPOGL
92.3 Cold shock protein CspB Q816H3 CSPD_BACCR
92.3 Cold shock protein CspB Q81K90 CSPD_BACAN
100.0 Cold shock protein CspB P32081 CSPB_BACSU