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• W2028499577 startingPage "2144" @default.
• W2028499577 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." @default.
• W2028499577 created "2016-06-24" @default.
• W2028499577 creator A5041775175 @default.
• W2028499577 creator A5056229406 @default.
• W2028499577 date "1994-11-01" @default.
• W2028499577 modified "2023-10-16" @default.
• W2028499577 title "Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from<i>Bacillus subtilis</i>" @default.
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• W2028499577 doi "https://doi.org/10.1002/pro.5560031127" @default.
• W2028499577 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2142648" @default.
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