Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of nonnative structure in the denatured state

Proteins: Structure, Function and Genetics

Volumn 38, Issue 2, 2000, Pages 189-196

  Demarest, Stephen J ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

lactalbumin; Denatured state; Molten globule state; Nonnative interactions; Trifluoroethanol

Indexed keywords

ALPHA LACTALBUMIN; TRIFLUOROETHANOL;

AQUEOUS SOLUTION; ARTICLE; HYDROPHOBICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS;

CIRCULAR DICHROISM; HUMANS; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 0034141812     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000201)38:2<189::AID-PROT7>3.0.CO;2-F     Document Type: Article

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