Santucci R, Giartosio A, Ascoli F
Department of Biochemical Sciences, University La Sapienza, Rome, Italy.
Arch Biochem Biophys. 1989 Dec;275(2):496-504. doi: 10.1016/0003-9861(89)90396-2.
Circular dichroism and differential scanning calorimetry studies on the unfolding-refolding process of native and carboxymethylated cytochrome c, induced either by temperature or chemical agents, have been performed. The results have shown that the modified protein has a decreased conformational stability with respect to the native state, in agreement with a structure less compact, but still highly folded, which behaves as a thermodynamically stable "intermediate" between native and fully unfolded cytochrome c.
