Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR

Biochemistry

Volumn 43, Issue 43, 2004, Pages 13775-13786

  Bann, James G ^a,b   Frieden, Carl ^a  

^a WASHINGTON UNIVERSITY   (United States)

^b WICHITA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONCENTRATION (PROCESS); FLUORESCENCE; ISOMERIZATION; KINETIC ENERGY; NUCLEAR MAGNETIC RESONANCE; PROTEINS; UREA;

DOMAIN-DOMAIN INTERACTIONS; UREA CONCENTRATION;

BACTERIA;

BACTERIAL PROTEIN; CHAPERONE; PHENYLALANINE; PROLINE; PROTEIN PAPD; UNCLASSIFIED DRUG; UREA;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; DENATURATION; FLUORESCENCE; ISOMERIZATION; ISOTOPE LABELING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION;

CIRCULAR DICHROISM; ESCHERICHIA COLI PROTEINS; FLUORINE; KINETICS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; P-FLUOROPHENYLALANINE; PEPTIDE FRAGMENTS; PERIPLASMIC PROTEINS; PHENYLALANINE; PROLINE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; STEREOISOMERISM; UREA;

BACTERIA (MICROORGANISMS);

EID: 7244229512     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048614u     Document Type: Article

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