The conformational stability of the Cold shock protein A (CspA) from C. pseudotuberculosis
(Cp), a nucleic acid binding protein in function of pH and salt concentration was examined by
using differential scanning calorimetry and CD spectroscopy in combination with computational
analysis to identify the specify amino acids undergoing change. Our approach identified a sodiumbinding
site in CpCspA and at pH 8.0 a significant reduction in the β-sheet content was observed
which resulted in a decrease of the protein thermal stability. The computational analyses identified
His30 and His65 as the amino acids with the largest charge shifts at different pHs. His30/His65 are
part of the extensive hydrogen bonding network and along with the ion-binding site are essential for
the conformational stability of CspA.
Keywords: Cold shock protein, C. pseudotuberculosis, ion binding, histidine, pH, secondary structure.
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