Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1926446 | Archives of Biochemistry and Biophysics | 2009 | 9 Pages |
Abstract
The folding properties of a bile acid binding protein, belonging to a subfamily of the fatty acid binding proteins, have been here investigated both by hydrogen exchange measurements, using the SOFAST NMR approach, and urea denaturation experiments. The urea unfolding profiles of individual residues, acting as single probes, were simultaneously analyzed through a global fit, according to a two-state unfolding model. The resulting conformational stability ÎGU(H2O) = 7.2 ± 0.25 kcal molâ1 is in good agreement with hydrogen exchange stability ÎGop. While the majority of protein residues satisfy this model, few amino-acids display a singular behavior, not directly amenable to the presence of a folding intermediate, as reported for other fatty acid binding proteins. These residues are part of a protein patch characterized by enhanced plasticity. To explain this singular behavior a tentative model has been proposed which takes into account the interplay between the dynamic features and the formation of transient aggregates. A functional role for this plasticity, related to translocation across the nuclear membrane, is discussed.
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Authors
Mariapina D'Onofrio, Laura Ragona, Dimitrios Fessas, Marco Signorelli, Raffaella Ugolini, Massimo Pedò, Michael Assfalg, Henriette Molinari,