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Determination of Membrane Protein Structure and Dynamics by Magic-Angle-Spinning Solid-State NMR Spectroscopy

2005; American Chemical Society; Volume: 127; Issue: 37 Linguagem: Inglês

10.1021/ja0530164

1943-2984

Ovidiu C. Andronesi, Stefan Becker, Karsten Seidel, Henrike Heise, Howard S. Young, Marc Baldus,

DNA and Nucleic Acid Chemistry

It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments are combined with novel through-bond correlation schemes that probe mobile protein segments. These NMR schemes are demonstrated on a uniformly [13C,15N] variant of the 52-residue polypeptide phospholamban. When reconstituted in lipid bilayers, the NMR data are consistent with an α-helical trans-membrane segment and a cytoplasmic domain that exhibits a high degree of structural disorder.