Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5

Protein Science

Volumn 10, Issue 5, 2001, Pages 1079-1083

  Chen, J ^a   Smith, D L ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

Amide hydrogen exchange; Malate dehydrogenase; Mass spectrometry

Indexed keywords

AMIDE; CHAPERONIN; DEUTERIUM; HYDROGEN; MALATE DEHYDROGENASE; MONOMER; PEPSIN A;

ARTICLE; ENZYME ANALYSIS; MASS SPECTROMETRY; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTON TRANSPORT;

AMIDES; DEUTERIUM; DIMERIZATION; GROEL PROTEIN; HYDROGEN-ION CONCENTRATION; KINETICS; MALATE DEHYDROGENASE; MASS SPECTROMETRY; MODELS, MOLECULAR; PEPSIN A; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS;

EID: 0035061716     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.53201     Document Type: Article

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