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Volumn 40, Issue 32, 2001, Pages 9623-9630
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A two-process model describes the hydrogen exchange behavior of cytochrome c in the molten globule state with various extents of acetylation
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Author keywords
[No Author keywords available]
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Indexed keywords
HYDROGEN EXCHANGE;
ACETYLATION;
HYDROGEN;
HYDROGEN BONDS;
MASS SPECTROMETRY;
PROTEINS;
PROTONS;
BIOCHEMISTRY;
ACETIC ACID DERIVATIVE;
AMIDE;
CYTOCHROME C;
DEUTERIUM;
HYDROCHLORIC ACID;
LYSINE;
PROTON;
ACETYLATION;
ARTICLE;
CIRCULAR DICHROISM;
CONTROLLED STUDY;
HYDROGEN BOND;
MASS SPECTROMETRY;
MODEL;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN SECONDARY STRUCTURE;
PROTEIN STABILITY;
PROTON TRANSPORT;
TRANSPORT KINETICS;
ACETYLATION;
ANIMALS;
CIRCULAR DICHROISM;
CYTOCHROME C GROUP;
HORSES;
HYDROGEN;
KINETICS;
PROTEIN CONFORMATION;
SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;
EQUUS CABALLUS;
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EID: 0035859878
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi002762c Document Type: Article |
Times cited : (10)
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References (42)
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