KCSA REVERSE MICELLE CB EXPERIMENT

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Integral membrane proteins play essential roles in a wide array ofbiological processes including nerve action potentials, homeostasis, cellarchitecture, and signal transduction. They comprise over 50% of currentand potential drug targets, yet their structural characterization haslagged far behind that of soluble proteins. For solution nuclear magneticresonance (NMR) spectroscopy, membrane proteins represent a significantchallenge because their solubilization in aqueous detergent micellesresults in particles of large size and attendant slow molecularreorientation. This limits the complexity of spectroscopy that can beemployed. We have developed a novel procedure for solubilizing membrane proteins in a surfactant system suitable for dissolution in low viscosity solvents such as pentane, butane, or propane, and are in the process of collecting 3D data for backbone assignments.