Comparison of the folding mechanism of highly homologous proteins in the lipid-binding protein family

Proteins: Structure, Function and Bioinformatics

Volumn 75, Issue 4, 2009, Pages 799-806

  Ropson, Ira J ^a   Boyer, Joshua A ^a,b   Schaeffer, Blake A ^a,c   Dalessio, Paula M ^a  

^a PENN STATE COLLEGE OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c U S ENVIRONMENTAL PROTECTION AGENCY   (United States)

Author keywords

sheet; Fluorine NMR; Folding initiation; Kinetics; Molten globule; Protein denaturation

Indexed keywords

HUMAN BILE ACID BINDING PROTEIN; LIPID BINDING PROTEIN; RAT BILE ACID BINDING PROTEIN; UNCLASSIFIED DRUG; UREA;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE; FLUORINE NUCLEAR MAGNETIC RESONANCE; HUMAN; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; RAT; SEQUENCE HOMOLOGY;

ANIMALS; CARRIER PROTEINS; HUMANS; HYDROXYSTEROID DEHYDROGENASES; KINETICS; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RATS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRYPTOPHAN; TYROSINE; UREA;

RATTUS;

EID: 66149164339     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22286     Document Type: Article

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