Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis.


Abstract

The intermolecular interactions of the major cold-shock protein from Bacillus subtilis (CspB) in solution in the presence of different salts, including phosphate, have been studied by means of scanning calorimetry and size-exclusion chromatography. Calorimetric results indicate that, in all cases, protein unfolding can be approximated by a 2-state model, but the modes of unfolding can differ depending on the conditions. In the presence of phosphate, the cooperative folding unit is a monomer, whereas in the absence of phosphate, the cooperative unit is a dimer. The difference in the self-association of CspB in the presence and absence of phosphate was supported by size-exclusion chromatography. These results are compared with recent structural studies of CspB in crystal and in solution. Study holds ProTherm entries: 11719, 11720, 11721, 11722, 11723, 11724, 11725 Extra Details: cold-shock protein; monomer-dimer; phosphate;,scanning microcalorimetry; size-exclusion chromatography

Submission Details

ID: eNN9KqMQ3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:43 p.m.

Version: 1

Publication Details
Makhatadze GI;Marahiel MA,Protein Sci. (1994) Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. PMID:7703860
Additional Information

Study Summary

Number of data points 21
Proteins Cold shock protein CspB ; Cold shock protein CspB
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: dHcal buffers:glycine/sodium-phosphate: 30 mM/50 mM, pH:9.0 ; Experimental Assay: Tm buffers:glycine/sodium-phosphate: 30 mM/50 mM, pH:9.0 ; Experimental Assay: dHvH buffers:glycine/sodium-phosphate: 30 mM/50 mM, pH:9.0 ; Experimental Assay: dHcal buffers:glycine: 30 mM, pH:9.0 ; Experimental Assay: Tm buffers:glycine: 30 mM, pH:9.0 ; Experimental Assay: dHvH buffers:glycine: 30 mM, pH:9.0 ; Experimental Assay: dHcal buffers:Sodium phosphate: 50 mM, pH:8.0 ; Experimental Assay: Tm buffers:Sodium phosphate: 50 mM, pH:8.0 ; Experimental Assay: dHvH buffers:Sodium phosphate: 50 mM, pH:8.0 ; Experimental Assay: dHcal buffers:Tris: 50 mM, pH:8.0 ; Experimental Assay: Tm buffers:Tris: 50 mM, pH:8.0 ; Experimental Assay: dHvH buffers:Tris: 50 mM, pH:8.0 ; Experimental Assay: dHcal pH:7.5, buffers:Sodium phosphate: 50 mM ; Experimental Assay: Tm pH:7.5, buffers:Sodium phosphate: 50 mM ; Experimental Assay: dHvH pH:7.5, buffers:Sodium phosphate: 50 mM ; Experimental Assay: dHcal buffers:imidazole: 50 mM, pH:7.5 ; Experimental Assay: Tm buffers:imidazole: 50 mM, pH:7.5 ; Experimental Assay: dHvH buffers:imidazole: 50 mM, pH:7.5 ; Experimental Assay: dHcal pH:7.5, buffers:HEPES: 50 mM ; Experimental Assay: Tm pH:7.5, buffers:HEPES: 50 mM ; Experimental Assay: dHvH pH:7.5, buffers:HEPES: 50 mM
Libraries Mutations for sequence MLEGKVKWFNSEKGFGFIEVEGQDDVFVHFSAIQGEGFKTLEEGQAVSFEIVEGNRGPQAANVTKEA

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 UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
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