Montana State University

Department of Chemistry and Biochemistry

Edward Dratz
Biochemistry, Biological Signaling Mechanisms and Global Proteomic Analysis

Edward Dratz

Professor
Office: Room251 Chemistry and Biochemistry Building
Lab: Room 244 Chemistry and Biochemistry Building

P.O. Box 173400
Bozeman, MT 59717
Ph: 406-994-4041
Fax: 406-994-5407
dratz@chemistry.montana.edu
Research Summary

B.A., Carleton College, 1961; Ph.D., University of California at Berkeley, 1966; Postdoctoral, University of California, Berkeley, 1966-67; Postdoctoral, Massachusetts Institute of Technology, 1967-69.

Courses:
· BCH 104RN THE BIOCHEMISTRY OF HEALTH FOR NON-SCIENCE MAJORS
· BCH 442 METABOLIC REGULATION

Awards and Professional Activities:
Helen Hay Whitney Postdoctoral Fellow, 1966-69; NATO International Travel Fellow, 1975-80; European Molecular Biology Organization Senior Fellow, 1981-83; Charles and Nora Wiley Award for Meritorious Research and Creativity, 1995; Sabbatical Fellowship to Harvard Medical School and MIT, 1996-97 and to the National Proteomics Center at the Medical College of Wisconsin 2003-4.

Research Overview

The Dratz lab uses global proteomics and metabolomics to investigate signaling networks in cells, animals and humans. We are applying proteomics and metabolic technology to finding new early warning diagnostics for type 2 diabetes, to better understand Alzheimer's Disease, the triggering mechanisms human epilepsy, and reprogramming of adult human cells into induced pluripotent stem cells (hiPSCs). We are developing new fluorescent reporters for measuring metabolite levels in living cells in real time, that show great promise for optimizing the hiPSC reprogramming process and thus increasing the practicality of regenerative medicine, promise to improve stem cell function in individual humans, and for providing new insights in many other states of health and disease . Prof. Dratz has a long standing interest in biochemical nutrition and is applying proteomic and metabolomic methods to gain deeper understanding of nutritional issues in human health and preventative medicine, in collaboration with researchers in Plant Sciences and Health and Human Developmetnt. We are also investigating the use of the volatile metabolites in human breath as non-invasive reporters of metabolic health.

The genome of an organism is quite static (apart from rare mutations), whereas the proteins expressed or modified by cells often change rapidly in response to stimuli and cellular metabolism tends to respond even faster. Proteins typically contain many different post-translational modifications (PTMs), which affect a protein's activity, cellular localization, or teaming with protein partners. Proteomics technology uses mass spectrometers for protein identification and for characterization of PTMs, but first must rely on a variety of separation techniques such as 2D gels (e.g. Halligan, et al., Nucleic Acids Res. 2004;32: W638-44) or liquid chromatography to separate complex protein or peptide mixtures before mass spectral analysis. We have been developing and testing novel, designer fluorescent dyes, in collaboration with others in the Department, that enhance detection sensitivity, pinpoint posttranslational modifications, and monitor changes in enzyme activity in the proteome. The metabolome is close to the phenotype of cells and thus studies of the metabolome can often greatly increase our understand of cellular responses in health and disease. Proteomics and metabolomics are major research frontiers in biological R&D and there are abundant research opportunities in bioanalytical chemistry, biochemistry, molecular biology and collaborations in chemical biology or cell biology for students trained in proteomics and/or metabolomics.

Selected Publications

Sands DC, Morris CE, Dratz EA, Pilgeram AL:
Elevating optimal human nutrition to a central goal of plant breeding and production of plant-based foods
Plant Science 177 (2009) 377–389

Piscitelli CL, Angel TE, Bailey BW, Hargrave P, Dratz EA, Lawrence CM. :
The equilibrium between metarhodopsin-I and metarhodopsin-II is dependent on the conformation of the 3rd cytoplasmic loop.
J Biol Chem. 2005 Dec 29

Riesselman M, Miettinen HM, Gripentrog JM, Lord CI, Mumey B, Dratz EA, Stie J,Taylor RM, Jesaitis AJ.:
C-terminal tail phosphorylation of N-formyl peptide receptor: differential recognition of two neutrophil chemoattractant receptors by monoclonal antibodies NFPR1 and NFPR2.
J Immunol. 179(4):2520-31, (2007).

Halligan BD, Ruotti V, Jin W, Laffoon S, Twigger SN, Dratz EA. :
ProMoST (Protein Modification Screening Tool): a web-based tool for mapping protein modifications on two-dimensional gels.
Nucleic Acids Res. 2004 Jul 1;32(Web Server issue):W638-44.

Barry RC, Alsaker BL, Robison-Cox JF, Dratz EA. :
Quantitative evaluation of sample application methods for semipreparative separations of basic proteins by two-dimensional gel electrophoresis.
Electrophoresis. 2003 Oct;24(19-20):3390-404.

Keywords:
Proteomics, Protein Chemistry, Chemical Biology



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