Abstract
Heteronuclear saturation transfer difference (STD) in high-resolution magic angle spinning (HR-MAS) NMR spectroscopy was applied to lipidic cubic phase (LCP) samples containing monoolein, cholesterol and a G-protein coupled receptor, the beta2 adrenergic receptor (beta2AR), in order to characterize the cholesterol beta2AR interactions. Previous evidence from thermal denaturation experiments and from the observation of conserved binding sites in crystal structures of the beta2AR suggested that cholesterol interacts with the beta2AR with high specificity.By analyzing 13C chemical shifts variations, STD intensities and 13C T1 relaxation times over a broad range of cholesterol concentration, we have demonstrated that the cholesterol- beta2AR interaction is real, but of very weak affinity.
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