Abstract
Denaturation temperatures (Td) and denaturation enthalpies (ΔH) for α-subunits from Escherichia coli, Salmonella typhimurium, and an interspecies hybrid in which the C-terminal domain comes from E. coli and N-terminal domain comes from S. typhimurium were determined by scanning microcalorimetry (DASM4) at various pH values. The Td of the E. coli protein was the highest at each pH and the Td of the hybrid protein was close to that of S. typhimurium. ΔH values of the three proteins were similar to each other at the same temperature. The results suggest that the difference in the stabilities between E. coli and S. typhimurium proteins is caused by the difference of hydrophobicity with replacements of Val to Ile at positions 52 and 166, which are buried in the interior of the molecule.
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