Noncooperative formation of the off-pathway molten globule during folding of the α-β parallel protein Apoflavodoxin

Journal of the American Chemical Society

Volumn 131, Issue 7, 2009, Pages 2739-2746

  Nabuurs, Sanne M ^a   Westphal, Adrie H ^a   Van Mierlo, Carlo P M ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

DENATURANT CONCENTRATION; DETRIMENTAL EFFECTS; FLAVODOXIN; FOLDING TRANSITION; GUANIDINIUM HYDROCHLORIDE; MOLTEN GLOBULE; MOLTEN GLOBULE STATE; NATIVE STATE; NATIVE STRUCTURES; NMR SPECTROSCOPY; RANDOM COIL; RESIDUE LEVEL; SECONDARY STRUCTURES; SIDE-CHAIN; STRUCTURE FORMATIONS; TRACK CHANGES; TRYPTOPHAN SIDE CHAIN; UNFOLDED PROTEINS;

AMIDES; AMINO ACIDS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

PROTEIN FOLDING;

FLAVODOXIN; GLOBULAR PROTEIN; MOLTEN GLOBULE; UNCLASSIFIED DRUG; ALANINE; APOFLAVODOXIN; APOPROTEIN; CYSTEINE;

ARTICLE; AZOTOBACTER VINELANDII; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; AMINO ACID SUBSTITUTION; CHEMISTRY; ISOLATION AND PURIFICATION; KINETICS; NUCLEAR MAGNETIC RESONANCE; PROCEDURES; PROTEIN DENATURATION; THERMODYNAMICS;

ALANINE; AMINO ACID SUBSTITUTION; APOPROTEINS; AZOTOBACTER VINELANDII; CYSTEINE; FLAVODOXIN; KINETICS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 67749133718     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja8089476     Document Type: Article

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