Protein Structure Core

自1988年以来，蛋白质结构核心一直是UM-MAC/RDCC的一部分。我们计划

The Protein Structure Core has been part of the UM-MAC/RDCC continuously since 1988. We plan to continue to provide timely and cost-efficient access to state-of-the-art protein biotechnology for RDCC members backed up by our exptertise in project planning, data analysis, and training. We will maintain our strong focus on interaction with RDCC investigators. While investigators are free to submit service requests without discussion, we encourage meetings with the Core Director for the purpose of efficient and practical planning, and for data analysis at the conclusion of a project. Peptide synthesis is currently our most frequently requested service and we expect that this will continue unchanged. We synthesize linear peptides as well as multiply labeled peptides, cyclic peptides and peptides mimicking post-translational modifications. Peptides can be ordered with tailored characteristics containing natural amino acids or modified unnatural structural elements (biotin or other affinity labels, fluorochromes, donor-acceptor pairs, conformational constraints, phosphates) for structure-function studies, immunological assays, antibody production, intracellular trafficking, and other applications. Pepetides will be synthesized using Fmoc-solid phase methodology. Peptide synthesis is coupled with RP-HPLC based purification of peptides, and mass spectroscopic analysis to confirm correct synthesis. We will also continue to offer currently available services in protein analysis, including Edman sequence analysis (to identify N-terminal sequence tags, complementing LC/MS analysis), amino acid analysis (outsourced, used to characterize unknown proteins to determine strategies for proteolysis before LC/MS analysis, and to quantify proteins and characteize MAP peptides), and circular dichroism (to determine protein secondary structure, conformational stability, and conformational effects of peptide modification). Our capacity in protein analysis will be vastly improved by the addition of a Waters LC/MS UPLC Qtof Premier Tandem mass spectrometer, which will be used in conjuction with bioinformatics analysis, for identification or proteins by peptide-mass -fingerprinting and tandem mass spectroscopy. We will also utilize the sensitivity and resolution of this instrument for identification of post-translational modification of proteins (especially phosphorylation), an increasingly important area in biomedical research.