Protein Structure Core

University Of Michigan At Ann Arbor, Ann Arbor MI

Investigators

Linked publications & trials

Abstract

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