Michael Marty - MALDI mass spectrometry of membrane proteins in Nanodiscs.

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      Publication Details (including relevant citation   information): Marty,Michael T., Das,Aditi,   Sligar,Stephen G., Abstracts, Joint 46th Midwest and 39th   Great Lakes Regional Meeting of the American Chemical Society,   St. Louis, MO, United States, October 19-22,   2011, pp MWGL-554

      Abstract: Over the last decade, Nanodiscs have   emerged as a leading technol. for solubilizing membrane proteins   for structural, functional, and enzymic studies. Nanodiscs are   nanoscopic, self-assembled lipid bilayers encircled by membrane   scaffold protein (MSP) belts. They provide a platform for   analyzing membrane proteins in a native-like lipid membrane   environment and have been used with a wide range of anal.   techniques. Conventional methods for MALDI mass spectrometry of   full-length membrane proteins in Nanodiscs are severely limited   by strong MSP signal and weak signal from the membrane proteins.   This is likely due to higher concns. of MSP and interference from   lipids surrounding the protein. We present here an optimized   ultra-thin layer sample prepn. technique, which enhances membrane   protein signal and nearly entirely suppresses MSP signal. The   suppression effect is investigated further with different   matrixes, first shot MALDI expts., and MALDI mass spectrometry   imaging. We show that this method can be successfully applied to   Nanodiscs contg. membrane proteins of different sizes and   membrane topologies, and we apply this ultra-thin layer method to   mixts. of membrane proteins in Nanodiscs. These results   demonstrate the general applicability of this method and open new   possibilities for future structural and functional mass   spectrometry studies of membrane proteins in Nanodiscs. [on   SciFinder(R)]

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