DEVELOPMENT OF VHF EMR FOR METALLOPROTEIN RESEARCH

DESCRIPTION: (Adapted from the applicant's abstract) Metals in metalloproteins plan key roles in protein structure and/or activity: small molecule binding/transport, substrate or cofactor binding, etc. Characterization of the metal centers provides crucial insight into biophysical and biochemical processes. These insights will prove invaluable in biomedicine and health care. Electron Magnetic Resonance (EMR) spectroscopy is potentially a unique and powerful tool for detecting and characterizing paramagnetic (metal) center in metalloproteins. Spin-physics of these metals -- high zero-field splittings, large nuclear quadrapoles and rapid relaxation -- make it difficult if not impossible to study these centers by "traditional" fields and frequencies (0.35 Tesla, 9.5 GHz). Very high field EMR with 10-25 times higher fields and frequencies promises to overcome these difficulties. The long-term goal is the characterization of paramagnetic centers in metalloproteins. Double resonance and pulsed techniques need to be developed. Work must be done on basic sensitivity and sample environs. The aim of Phase I is the development of requisite superconducting-magnet, field controls to support further stages for the research. Control is required for precision, multi-Tesla sweeps and actively- stable, fixed-field operation. This technology is not commercially available and prototype systems in academia are inadequate to the task. $ = TOTAL AWARD AMTS & NOT LIMITED TO PORTION OF PROJECT RELATED TO SUBJECT OF SEARCH SUBPROJECT $ = TOTAL AWARD AMOUNT DIVIDED BY NUMBER OF SUBPROJECTS SOURCE: CRISP FORMAT F FY 97 LAST UPDATE 04-07-98 1QUERY 1536 ID SEARCH 06/01/98 PAGE 319 --PROJECT NUMBER......2 R44 GM54110-02 INVESTIGATOR NAME/ADDRESS FY 97 GARRELS, JAMES I IRG/INTRAMURAL UNIT..ZRG3 PROTEOME, INC AWARD AMOUNT......... $374,863 200 CUMMINGS CTR, SUITE 425C BEVERLY, MA 01915 PERFORMING ORGANIZATION: PROTEOME, INC. TITLE COMPREHENSIVE PROTEIN DATABASE FOR YEAST S CEREVISIAE ABSTRACT: A proteome database, containing properties and functions for all the proteins coded by a genome, has been built for the yeast Saccharomyces cerevisiae. The Yeast Protein Database (YPD) contains a page (YPD Protein Report) on the WWW (www.proteome.com/YPDhome.html) for each of the 6000 yeast proteins. The information sources for YPD are the genome sequence and the yeast literature, of which 3000 papers have been reviewed. In the next two years, the literature review for yeast proteins will be completed and new information services will be developed, including an enhanced WWW presentation (YPD-Plus) and an automatic notification service. The latter service will alert users to new information within their interest profile and will automatically deliver the information in a user-specified format. Finally, a new level of information presentation, the YPD Protein Minireviews, will be implemented to summarize and extend the information presented in the YPD Protein Reports. These minireviews, each written by an expert author, will contain graphics and hypertext links to YPD Protein Reports, other databases, and Medline abstracts. The platform of YPD Protein Reports and YPD Protein Minireviews will constitute a comprehensive information resource of commercial value regarding the proteome of an important model organism. In the modern fields of genomics and proteomics, model organism data is constantly used to add functional information to new human gene and protein sequences.