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- W1973047305 abstract "We present a spectroscopic and calorimetric study on the thermal denaturation of bovine β-lactoglobulin (β-lg) variant A. Spectroscopic data allowed detection of a stable intermediate emerging from structural modifications restricted to local regions of the native molecule. It is suggested that this kind of intermediate could be a common property of lipocalins. Using the same set of parameters that has successfully related thermodynamics and structural properties of other proteins, it is shown that the thermally denatured state of β-lg retains a significant amount of buried hydrophobic surface area. Thus, despite being a small protein composed of a single structural domain, β-lg exhibits a complex unfolding mechanism, comprising at least two other species different from the native and completely unfolded states." @default.
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- W1973047305 date "1998-07-01" @default.
- W1973047305 modified "2023-10-18" @default.
- W1973047305 title "Spectroscopic and thermodynamic evidence for a complex denaturation mechanism of bovine β-lactoglobulin A" @default.
- W1973047305 doi "https://doi.org/10.1080/15216549800203172" @default.
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