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

H. Kenney Basehore, Ira Ropson

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by 19F NMR. Equilibrium unfolding studies of BABP labeled with fluorine at all eight of its phenylalanine residues showed that at least two sites experience changes in solvent exposure at high denaturant concentrations. Peak assignments were made by site-specific 4FPhe incorporation. The resonances for proteins specifically labeled at Phe17, Phe47, and Phe63 showed changes in chemical shift at denaturant concentrations at which the remaining five phenylalanine residues appear to be fully solvent-exposed. Phe17 is a helical residue that was not expected to participate in a folding initiation site. Phe47 and Phe63 form part of a hydrophobic core region that may be conserved as a site for folding initiation in the intracellular lipid-binding protein family. Published by Wiley-Blackwell.

Original languageEnglish (US)
Pages (from-to)327-335
Number of pages9
JournalProtein Science
Volume20
Issue number2
DOIs
StatePublished - Feb 1 2011

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Phenylalanine
Nuclear magnetic resonance
Fluorine
Chemical shift
Carrier Proteins
Lipids
Proteins
bile acid binding proteins
human AKR1C2 protein

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Basehore, H. Kenney ; Ropson, Ira. / Residual interactions in unfolded bile acid-binding protein by 19F NMR. In: Protein Science. 2011 ; Vol. 20, No. 2. pp. 327-335.
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Residual interactions in unfolded bile acid-binding protein by 19F NMR. / Basehore, H. Kenney; Ropson, Ira.

In: Protein Science, Vol. 20, No. 2, 01.02.2011, p. 327-335.

Research output: Contribution to journalArticle

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