Extensive formation of off-pathway species during folding of an α-β parallel protein is due to docking of (non)native structure elements in unfolded molecules

Journal of the American Chemical Society

Volumn 130, Issue 50, 2008, Pages 16914-16920

  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

AGGREGATION PHENOMENONS; AMINO ACID RESIDUES; CONFORMATIONAL PREORGANIZATION; FOLDING INTERMEDIATES; GUANIDINE HYDROCHLORIDES; HETERONUCLEAR; HYDROPHOBIC INTERACTIONS; NANO-SECONDS; NATIVE PROTEINS; NATIVE STRUCTURES; NMR SPECTROSCOPIES; RANDOM COILS; RELAXATION RATES; RESIDUE LEVELS; TIME SCALES;

AMINES; AMINO ACIDS; FORMING; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC ACIDS;

PROTEIN FOLDING;

APOPROTEINS; AZOTOBACTER VINELANDII; CIRCULAR DICHROISM; FLAVODOXIN; GUANIDINE; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 58049200780     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja803841n     Document Type: Article

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