The biological functions and molecular structures of proteins are highly dependent on the physical and chemical properties of the surrounding environment. Just as water is essential for supporting the native states of soluble proteins, the lipid bilayer is critical for preserving the functional and structural integrity of membrane proteins. The principal advantage of NMR spectroscopy as a method for structure determination is its ability to examine proteins in samples that are very close to their functional environments. NMR is well suited for studying soluble proteins in water and membrane proteins in lipid bilayer environments. We will describe recent progress on NMR structural studies of two membrane proteins that play key roles in bacterial human infection and in regulation of human programmed cell death. Optimized samples enable high resolution NMR spectra to be obtained in detergent-free membranes. New computational methods, designed specifically for proteins in membranes, enhance structural accuracy. Parallel structural and activity studies on identical samples shed light on the biological functions of the protein-membrane assembly.<br/><br/>Supported by grants from the National Institutes of Health (GM118186, CA179087). It utilized the NIH-supported NMR Facilities at the Sanford-Burnham Medical Research Institute (CA030199) and at the University of California San Diego (EB002031).

NMR structure and function of membrane proteins in membranes

254th National Meeting (2017)

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