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Volumn 268, Issue 16, 2001, Pages 4537-4543
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Cytochrome c reconstituted from two peptide fragments displays native-like redox properties
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Author keywords
Circular dichroism; Cyclic voltammetry; Cytochrome c; Fragment recombination; Redox potential
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Indexed keywords
CYTOCHROME C;
CYTOCHROME C OXIDASE;
FERRIC ION;
PEPTIDE FRAGMENT;
ALPHA HELIX;
ARTICLE;
ENZYME MECHANISM;
ENZYME RECONSTITUTION;
OXIDATION REDUCTION POTENTIAL;
PH;
PH ELECTRODE;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN CROSS LINKING;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
ANIMALS;
CIRCULAR DICHROISM;
CYTOCHROME C GROUP;
ENZYME STABILITY;
HORSES;
OXIDATION-REDUCTION;
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EID: 0034831421
PISSN: 00142956
EISSN: None
Source Type: Journal
DOI: 10.1046/j.1432-1327.2001.02373.x Document Type: Article |
Times cited : (12)
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References (37)
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