A residual structure in unfolded intestinal fatty acid binding protein consists of amino acids that are neighbors in the native state

Biochemistry

Volumn 45, Issue 8, 2006, Pages 2608-2617

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

^a PENN STATE COLLEGE OF MEDICINE   (United States)

^b University of North Carolina ^*  (United States)

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

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CARBOXYLIC ACIDS; FATTY ACIDS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; RESIDUAL STRESSES;

AROMATIC AMINO ACIDS; DYNAMIC BEHAVIOR; INTESTINAL FATTY ACID BINDING PROTEIN (IFABP); RESIDUAL STRUCTURES;

PROTEINS;

AMINO ACID; FATTY ACID BINDING PROTEIN; FLUORINE; PHENYLALANINE; TRYPTOPHAN; TYROSINE; UREA;

ARTICLE; BETA SHEET; CIRCULAR DICHROISM; ESCHERICHIA COLI; FLUORESCENCE; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

AMINO ACIDS; CIRCULAR DICHROISM; FATTY ACID-BINDING PROTEINS; FLUORESCENCE; FLUORINE; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHENYLALANINE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; TRYPTOPHAN; TYROSINE; UREA;

ESCHERICHIA COLI;

EID: 33644502195     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052091o     Document Type: Article

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