Protein Structure Core

蛋白质结构核心

基本信息

批准号：
7662387
负责人：
HENRIETTE Anna REMMER
金额：
$ 5.32万
依托单位：
UNIVERSITY OF MICHIGAN AT ANN ARBOR
依托单位国家：
美国
项目类别：
财政年份：
2008
资助国家：
美国
起止时间：
2008-08-01 至 2011-07-31
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/7662387
关键词：
Affinity Labels Amino Acids Antibody Formation Area Arts Back Bioinformatics Biological Assay Biomedical Research Biotechnology Biotin Characteristics Circular Dichroism Circular Dichroism Spectroscopy Complement Core Protein Coupled Custom Cyclic Peptides Data Analyses Elements Fingerprint Fluorochrome Goals Label Mass Spectrum Analysis Methodology Modification N-terminal Outsourcing Peptide Synthesis Peptides Phase Phosphorylation Post-Translational Protein Processing Protein Analysis Proteins Proteolysis Purpose Research Personnel Resolution Secondary Protein Structure Sequence Analysis Services Solid Structure Training Water affinity labeling base cost improved inorganic phosphate instrument intracellular protein transport liquid chromatography mass spectrometry mass spectrometer member protein localization location protein structure trafficking

项目摘要

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.