Abstract
Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a near-native lipid bilayer environment. The main limitation of the method is spectral resolution and sensitivity, however recent developments in ssNMR hardware, including the commercialization of 28 T magnets (1.2 GHz proton frequency) and ultrafast MAS spinning (<100 kHz) promise to accelerate acquisition, while reducing sample requirement, both of which are critical to membrane protein studies. Here, we review recent advances in ssNMR methodology used for structure determination of membrane proteins in native and mimetic environments, as well as the study of protein functions such as protein dynamics, and interactions with ligands, lipids and cholesterol.
Highlights
Membrane proteins (MPs) at the interface of cells and the cellular environment, or at the barrier separating cellular compartments, conduct a vast number of functions, such as signal transduction, metabolite transportation and energy conversion.[1]
Solid-state NMR is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a nearnative lipid bilayer environment
X-ray diffraction is capable of determining protein structure at a resolution higher than 2 A, and time resolved crystallography broadens its applicability from static structure determination to investigating dynamic aspects of protein function.[5]
Summary
Membrane proteins (MPs) at the interface of cells and the cellular environment, or at the barrier separating cellular compartments, conduct a vast number of functions, such as signal transduction, metabolite transportation and energy conversion.[1]. No single technique is effective across the wide array of different MPs, and there are o en signi cant discrepancies between structures determined by different methods if the protein's environment was far from a native lipid bilayer.[4]. X-ray diffraction is capable of determining protein structure at a resolution higher than 2 A, and time resolved crystallography broadens its applicability from static structure determination to investigating dynamic aspects of protein function.[5] Obtaining high quality crystals in the presence of detergent or lipid cubic phase remains challenging, .[6] Advances in single particle cryo-EM has led to an explosion in the number of structures available for large proteins (>50 kDa) and protein complexes. We show applications of ssNMR in the study of ligand binding, probing MP exposure to water or lipids, and determining protein dynamics
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