High-Resolution Solid-State NMR Spectroscopy of Membrane Bound Proteins and Peptides Aligned in Hydrated Lipids

Abstract

Abstract:

Solid-state nuclear magnetic resonance (NMR) of aligned samples has been rapidly -emerged as a successful and important spectroscopic approach for high-resolution structural characterization of membrane-bound proteins and peptides in their “native-like” hydrated lipid bilayers. Because the structures, dynamics, and functions of membrane-bound proteins and peptides are highly associated with heterogeneous native environments, proteins and peptides are prepared for solid-state NMR measurements in the presence of either bilayers that are mechanically aligned on glass plates or magnetically aligned bicelles. Orientation dependent anisotropic spin nuclear interactions from these aligned proteins and peptides can be obtained. These orientational restraints can be assembled into high-resolution threedimensional structures. Driven by significant advances in sample preparation protocols as well as NMR probes and other methodology developments in the past decade, the aligned sample NMR approach has been well developed and become an effective way for structural characterization of membrane-bound proteins and peptides. This review introduces high resolution solid-state NMR spectroscopy of aligned samples and summarizes recent methodology developments in this arena.

Key words: solid-state NMR, membrane-bound protein, orientational constraint, hydrated lipids

CLC Number:

O482.53

FU Ri-Qiang. High-Resolution Solid-State NMR Spectroscopy of Membrane Bound Proteins and Peptides Aligned in Hydrated Lipids[J]. Chinese Journal of Magnetic Resonance, 2009, 26(4): 437-456.

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