[Wide-angle x-ray scattering comparison of the structure of crystalline cytochrome c and cytochrome c in solution].
Large-angle X-ray diffuse scattering has been used for studying the conformational changes in cytochrome c during its transition from crystal into solution and during a change of the electron state of the heme. It has been found that the structure of cytochrome c in solution differs from its structure in crystal by a shift of the chain fragment in the region of 60-77 amino acid residues. The studies of the oxidized, reduced and cyanoforms of protein in solution have not revealed noticeable changes in the protein structure.
D055598:Chemical Phenomena; D002621:Chemistry; D003460:Crystallization; D003574:Cytochrome c Group; D004578:Electron Spin Resonance Spectroscopy; D010084:Oxidation-Reduction; D011487:Protein Conformation; D012542:Scattering, Radiation; D012996:Solutions; D014965:X-Rays
D003574:Cytochrome c Group; D012996:Solutions
Sravnenie struktury tsi tokhroma c v kristalle i rastvore metodom rasseianiia rentgenovskikh lucheĭ pod bol'shimi uglama.