Abstract
Abstract Bovine β -lactoglobulin is a globular protein that maintains a large solvent-exposed hydrophobic pocket, into which a variety of hydrophobic molecules, such as fatty acids, retinoids (e.g. vitamin A) and cholesterol, has been shown to bind. The protein, which belongs to the superfamily of lipocalins, comprises a very rigid eight-stranded primarily β -barrel core and a number of very flexible loops connecting the β strands. Protein three-dimensional structures derived from X-ray crystallographic and nuclear magnetic resonance spectroscopic studies are compared to ascertain intrinsic differences in the core structure under very different experimental conditions. A semi-quantitative model, based in part on surface free-energy minimization, is presented. It offers fresh insight into the critical structural role that the flexible loops play in providing entropic stabilization to the substantial entropic cost (∼100 kJ mol −1 ) of maintaining the large hydrophobic pocket.
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