ABSTRACT
ABSTRACT Solid-state NMR spectroscopy enables the structures of membrane peptides and proteins to be determined in lipid bilayers. Regardless of fold, all membrane proteins adopt three-dimensional structures with a unique direction in space defined by the membrane environment. Because this directionality is an intrinsic characteristic of membrane protein structure and function, it is highly desirable to carry out structure determination within the context of bilayer lipid membranes. Solid-state NMR spectroscopy of uniaxially oriented planar bilayer lipid samples is ideally suited for this purpose. This chapter outlines the methodology for membrane protein structure determination using solid-state NMR of oriented planar lipid bilayer samples. Recent developments in sample preparation, recombinant bacterial expression systems for the preparation of isotopically labeled membrane proteins, pulse sequences for high-resolution spectroscopy, and structural indices that guide the
structure assembly process, have greatly extended the capabilities of the technique, and are described. The methods are illustrated with examples from the FXYD proteins, a family of auxiliary regulatory subunits of the Na,K-ATPase.
