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

✍ Scribed by H. Kenney Basehore; Ira J. Ropson

Publisher: Cold Spring Harbor Laboratory Press
Year: 2011
Tongue: English
Weight: 663 KB
Volume: 20
Category: Article
ISSN: 0961-8368
DOI: 10.1002/pro.563

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✦ Synopsis

Abstract

The folding initiation mechanism of human bile acid‐binding protein (BABP) has been examined by ^19^F 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.

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