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

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
Sequence Assay Result Units