Folding subdomains of thioredoxin characterized by native-state hydrogen exchange

Protein Science

Volumn 12, Issue 8, 2003, Pages 1719-1731

  Bhutani, Nidhi ^a   Udgaonkar, Jayant B ^a  

^a UNIVERSITY OF AGRICULTURAL SCIENCES   (India)

Author keywords

Folding; Native state HX; NMR spectroscopy; Thioredoxin; Unfolded state

Indexed keywords

AMIDE; ESCHERICHIA COLI PROTEIN; GUANIDINE; HYDROGEN; PROTON; THIOREDOXIN;

ALPHA HELIX; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DEUTERIUM HYDROGEN EXCHANGE; DRUG EFFECT; HYDROGEN BOND; KINETICS; METABOLISM; METHODOLOGY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTON TRANSPORT; THERMODYNAMICS;

AMIDES; DEUTERIUM EXCHANGE MEASUREMENT; ESCHERICHIA COLI PROTEINS; GUANIDINE; HYDROGEN; HYDROGEN-ION CONCENTRATION; KINETICS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTONS; THERMODYNAMICS; THIOREDOXIN;

ESCHERICHIA COLI;

EID: 0042343673     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0239503     Document Type: Article

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