Proton NMR study of chemically modified horse heart ferricytochrome c confirms the presence of histidine and lysine-ligated conformers in 30% acetonitrile solution

Journal of Inorganic Biochemistry

Volumn 94, Issue 4, 2003, Pages 381-385

  Sivakolundu, Sivashankar G ^a   Mabrouk, Patricia Ann ^a  

^a NORTHEASTERN UNIVERSITY   (United States)

Author keywords

Alkaline transition; Histidine ligated cytochrome c; Lysine ligated cytochrome c; NMR; Protein folding

Indexed keywords

ACETONITRILE; CYTOCHROME C; HISTIDINE; HYDROXIDE; LYSINE; PLATINUM DERIVATIVE;

ARTICLE; CHEMICAL MODIFICATION; CONTROLLED STUDY; HEART; HORSE; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; ULTRAVIOLET SPECTROSCOPY;

ACETONITRILES; ANIMALS; CYTOCHROME C GROUP; GUANIDINES; HEME; HISTIDINE; HORSES; LIGANDS; LYSINE; MITOCHONDRIA, HEART; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; ORGANOPLATINUM COMPOUNDS; PROTEIN CONFORMATION; PROTONS; SOLUTIONS;

EQUUS CABALLUS;

EID: 0037379147     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0162-0134(03)00046-1     Document Type: Article

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