What question did this study set out to answer?

To examine how membrane proteins, polypeptides, and cholesterol alter phospholipid membrane structure and dynamics.

Phosphorus nuclear magnetic resonance study of membrane structure. Interactions of lipids with protein, polypeptide, and cholesterol.

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To examine how membrane proteins, polypeptides, and cholesterol alter phospholipid membrane structure and dynamics.
Acquired proton-decoupled 31P nuclear magnetic resonance spectra of lipid, lipid-protein, and lipid-cholesterol systems using Fourier transform at 60.7 MHz (3.52 Tesla).
Measured 31P chemical shielding anisotropy and determined spin-spin (T2) and spin-lattice (T1) relaxation rates above the gel-to-liquid crystal phase transition temperature.
Membrane proteins slightly decreased apparent 31P chemical shielding anisotropy above the lipid phase transition temperature.
Proteins significantly shortened 31P spin-spin (T2) and spin-lattice (T1) relaxation times, reflecting immobilization of the phospholipid headgroup via polar interactions.
Orientation strongly governed phospholipid T2 relaxation rates in both the presence and absence of proteins or cholesterol.

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Spectroscopic study demonstrates phospholipid headgroup immobilization in model lipid membranes, indicating direct polar interactions with proteins.

Rajan et al. (1981) studied this question.

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Spectroscopic study demonstrates phospholipid headgroup immobilization in model lipid membranes, indicating direct polar interactions with proteins.