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Volumn 99, Issue 2, 2002, Pages 709-714
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Real-time and equilibrium 19F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD
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Author keywords
Circular dichroism; Flourescence; Folding intermediates; P pili
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Indexed keywords
6 FLUOROTRYPTOPHAN;
CHAPERONE;
FLUORINE;
FLUORINE 18;
PROTEIN PAPD;
TRYPTOPHAN;
UNCLASSIFIED DRUG;
UREA;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CIRCULAR DICHROISM;
CONTROLLED STUDY;
ESCHERICHIA COLI;
FLUORESCENCE;
KINETICS;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN INTERACTION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
PYELONEPHRITIS;
STRAIN DIFFERENCE;
BACTERIAL PROTEINS;
BIOPHYSICS;
CIRCULAR DICHROISM;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
FLUORINE;
HUMANS;
MAGNETIC RESONANCE SPECTROSCOPY;
MOLECULAR CHAPERONES;
MUTAGENESIS, SITE-DIRECTED;
PERIPLASMIC PROTEINS;
PROTEIN FOLDING;
PROTEIN STRUCTURE, TERTIARY;
TRYPTOPHAN;
UREA;
ESCHERICHIA COLI;
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EID: 0037154219
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.022649599 Document Type: Article |
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Times cited : (61)
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References (27)
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