pH-dependent structural change of cytochrome-C
Egyptian Journal of Biomedical Engineering. 1994; 10: 1-10
en Inglés
| IMEMR
| ID: emr-106288
ABSTRACT
Effect of pH variation on the dynamic motion of cytochrome-C through conductivity, electronic absorption spectra and magnetic susceptibility coupled with molecular weight change were investigated. The very low pH region increases the probability of conversion native cytochrome-C to random coil. Neutralization leads to fold protein after being unfolded. Low spin state, mixture of low spin and high spin and high spin state of iron heme of cytochrome-C were demonstrated at acidic, neutral and alkali solution, respectively
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Índice:
IMEMR (Mediterraneo Oriental)
Asunto principal:
Concentración de Iones de Hidrógeno
Límite:
Animales
Idioma:
Inglés
Revista:
Egypt. J. Biomed. Eng.
Año:
1994
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