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Effect of pH and phosphate ions on self‐association properties of the major cold‐shock protein from Bacillus subtilis
Author(s) -
Makhatadze George I.,
Marahiel Mohamed A.
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560031127
Subject(s) - bacillus subtilis , phosphate , dimer , chemistry , size exclusion chromatography , intermolecular force , crystallography , monomer , protein folding , folding (dsp implementation) , calorimetry , chromatography , biophysics , biochemistry , molecule , polymer , thermodynamics , organic chemistry , biology , bacteria , genetics , physics , electrical engineering , enzyme , engineering
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.