Effect of pH on the Iso-1-cytochrome c denatured state: Changing constraints due to heme ligation

Biochemistry

Volumn 42, Issue 7, 2003, Pages 2174-2184

  Smith, Christopher R ^a   Wandschneider, Eydiejo ^a   Bowler, Bruce E ^a  

^a UNIVERSITY OF DENVER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LIGANDS;

MUTAGENESIS; PH EFFECTS; POLYPEPTIDES; QUENCHING;

BIOCHEMISTRY;

CYTOCHROME C; GUANIDINE; HEME; HISTIDINE; LYSINE;

ALKALINITY; ARTICLE; BINDING AFFINITY; ENERGY TRANSFER; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DENATURATION; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS;

ACETYLATION; AMINO ACID SUBSTITUTION; BINDING, COMPETITIVE; CYTOCHROME C GROUP; CYTOCHROMES C; GUANIDINE; HEME; HISTIDINE; HYDROGEN-ION CONCENTRATION; LIGANDS; LYSINE; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN; VARIATION (GENETICS);

EID: 0037465522     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026827i     Document Type: Article

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