Residual interactions in unfolded bile acid-binding protein by 19F NMR

Protein Science

Volumn 20, Issue 2, 2011, Pages 327-335

  Basehore, H Kenney ^a   Ropson, Ira J ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

Bile acid binding protein; Fluorine NMR; Hydrophobic collapse; Intestinal fatty acid binding protein; Protein folding; Residual structure; Unfolded proteins

Indexed keywords

BILE ACID BINDING PROTEIN; BINDING PROTEIN; PHENYLALANINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; FLUORINE NUCLEAR MAGNETIC RESONANCE; HUMAN; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

FLUORINE; HUMANS; HYDROXYSTEROID DEHYDROGENASES; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHENYLALANINE; PROTEIN FOLDING; RECOMBINANT PROTEINS; UREA;

EID: 79251560304     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.563     Document Type: Article

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