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Volumn 57, Issue 1, 2000, Pages 29-36
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Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies
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Author keywords
Circular dichroism; Cytochrome c; Heme ligation; Magnetic circular dichroism; Molten globule; Protein folding
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Indexed keywords
CYTOCHROME C OXIDASE;
FERRIC ION;
FERROUS ION;
HEME;
ABSORPTION SPECTROSCOPY;
ARTICLE;
CIRCULAR DICHROISM;
OXIDATION REDUCTION STATE;
PROTEIN FOLDING;
PROTEIN PROTEIN INTERACTION;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STABILITY;
PROTEIN TERTIARY STRUCTURE;
SPECTRAL SENSITIVITY;
ANIMALS;
CIRCULAR DICHROISM;
CYTOCHROME C GROUP;
HEME;
HORSES;
KINETICS;
OXIDATION-REDUCTION;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
SPECTROPHOTOMETRY;
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EID: 0034025695
PISSN: 00063525
EISSN: None
Source Type: Journal
DOI: 10.1002/(SICI)1097-0282(2000)57:1<29::AID-BIP5>3.0.CO;2-V Document Type: Article |
Times cited : (45)
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References (24)
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