title: Structural transitions of carboxymethylated cytochrome c: calorimetric and circular dichroic studies.
abstract: 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.
authors.affiliation: Department of Biochemical Sciences, University La Sapienza, Rome, Italy.
authors.forename: R
authors.initials: R
authors.lastname: Santucci
authors.forename: A
authors.initials: A
authors.lastname: Giartosio
authors.forename: F
authors.initials: F
authors.lastname: Ascoli
mesh_terms: D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D003574:Cytochrome c Group / Q000378:metabolism*; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D007700:Kinetics; D008715:Methionine; D008745:Methylation; D011487:Protein Conformation; D011489:Protein Denaturation; D014508:Urea / Q000494:pharmacology
chemical_list: D003574:Cytochrome c Group; D006146:Guanidines; D014508:Urea; D008715:Methionine; D019791:Guanidine