Abstract
ABSTRACTSolid-state nuclear magnetic resonance (SSNMR) is an NMR spectroscopy applied to condensed-phase systems, including membrane proteins. Membrane protein fold and function are dependent upon interactions with surrounding bilayer components. Structural and functional analyses are thus challenging, and new approaches are needed to better characterise these systems. SSNMR is uniquely suited to the examination of membrane proteins in native environments, and has the capabilities to elucidate complex protein mechanisms and structures. Notable research implementing SSNMR is aimed at developing new strategies and technology to efficiently target membrane proteins within synthetic and biological membranes. Significant advances have been made: observation of protein function in native environments, emergence of in situ methods to examine integral proteins within natural membranes, sensitivity enhancement techniques and cutting-edge structure determination methods. We present how these advances are applied to answer outstanding questions in structural biology. Experiments have shown consistent results for protein investigations in biological membranes and synthetic lipid compositions, indicating that SSNMR is an innovative and direct approach for the study of these systems.
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