Multiple roles of prolyl residues in structure and folding

Journal of Molecular Biology

Volumn 301, Issue 3, 2000, Pages 737-747

  Eyles, Stephen J ^a   Gierasch, Lila M ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

Circular dichroism; Conformational entropy; Fluorescence; Lipid binding proteins; Proline isomerization; Stability

Indexed keywords

ALANINE; LIPID BINDING PROTEIN; PROLINE DERIVATIVE; RETINOIC ACID BINDING PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATIONAL TRANSITION; ENTROPY; ISOMERISM; KINETICS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

EID: 0034682867     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4002     Document Type: Article

References (50)

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14. Protein conformational stability probed by Fourier transform ion cyclotron resonance mass spectrometry
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37. Turns in peptides and proteins
38. Refinement of the structure of Escherichia coli-derived rat intestinal fatty acid binding protein with bound oleate to 1.75 Å resolution. Correlation with the structures of the apoprotein -and the protein with bound palmitate
39. Unfolding free energy changes determined by the linear extrapolation method. 2. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
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