NATIVE & RECOMBINANT MEMBRANE PROTEINS FOR DETERMINING FUNCTION MECHANISM

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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. Our laboratory focus is to reveal functional mechanisms of integral membrane proteins, soluble proteins, and peptides at the level of chemistry and atomic structure for impact on drug design. Membrane proteins include many members of the GPCR, TRP, Aquaglycerol, Vglut, and Amt families. Soluble proteins include RNA processing enzymes, SRP proteins, Polyketide Synthases, EPO receptors, and designed helical bundles. Synthesized peptides include those used for antibody production, enzyme substrates and ligands, and peptitergents. Following expression and synthesis, these proteins and peptides will be purified and characterized prior to 3-D crystallization. To facilitate characterization and crystallization, mass spectrometry will be used to assay purity, mass, and post-translational processing events. In addition, these efforts will further develop purification procedures of hydrophobic proteins and peptides in environments amenable for mass spectrometry.