Related ArticlesResidual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Protein Sci. 2010 Nov 29;
Authors: Basehore HK, Ropson IJ
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.
PMID: 21117238 [PubMed - as supplied by publisher]
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Protein Sci. 2011 Feb;20(2):327-35
Authors: Basehore HK, Ropson IJ
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...
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Protein-DNA and protein-RNA complexes play key functional roles in every living organism. Therefore, the elucidation of their structure and dynamics is an important goal of structural and molecular biology. Nuclear magnetic resonance (NMR) studies of protein and nucleic acid complexes have common features with studies of protein-protein complexes: the...
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[NMR paper] Probing residual interactions in unfolded protein states using NMR spin relaxation te
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[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
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[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
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Theoretical framework for NMR residual dipolar couplings in unfolded proteins
Theoretical framework for NMR residual dipolar couplings in unfolded proteins
O. I. Obolensky, Kai Schlepckow, Harald Schwalbe and A. V. Solov’yov
Journal of Biomolecular NMR; 2007; 39(1) pp 1-16
Abstract:
A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arranged obstacles. For the case of bicelles oriented perpendicular to...
Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Linear Mode
