The stability of the cytochrome c scaffold as revealed by NMR spectroscopy

Journal of Inorganic Biochemistry

Volumn 98, Issue 5, 2004, Pages 814-823

  Berners Price, Susan J ^a   Bertini, Ivano ^b   Gray, Harry B ^c   Spyroulias, Georgios A ^d   Turano, Paola ^b  

^a UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

^b UNIVERSITY OF FLORENCE   (Italy)

^c CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

^d UNIVERSITY OF PATRAS   (Greece)

Author keywords

Cytochrome c; NMR spectroscopy; Unfolding

Indexed keywords

CYTOCHROME C; FERRIC ION; METHIONINE;

ALKALINITY; CONFERENCE PAPER; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; HORSE; METAL BINDING; MILK; MITOCHONDRION; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; YEAST;

ANIMALS; CYTOCHROMES C; HORSES; MODELS, MOLECULAR; MYOCARDIUM; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; SACCHAROMYCES CEREVISIAE PROTEINS;

EQUUS CABALLUS;

EID: 2342604894     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2003.12.010     Document Type: Conference Paper

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