Ronald L. Cerny
Associate Research Professor
Hamilton Hall 710
402.472.6020
rcerny1@unl.edu
Nebraska Center for Mass Spectrometry
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Current Research
Our research focus is on mass spectrometry. We are especially interested in the use of this technique to study and characterize biomolecules.
These studies include molecular weight determinations of intact proteins, determination of post-translational modifications and mapping potential binding sites for protein-protein and protein-drug interactions. We are also active in the rapidly expanding research area of proteomics.
Mass spectrometry is the method of choice for the identification of proteins isolated from biological systems. It is a very sensitive analytical technique, with the ability to detect low femtomole amounts of a compound.
We utilize a variety of ionization methods and mass analyzers in these proteomics studies. Protein identification can be accomplished by two different approaches. The first, peptide mapping, requires very accurate measurement of peptides. This requirement can be met by using matrix-assisted laser desorption ionization (MALDI) in conjunction with a time-of-flight mass spectrometer.
A second approach to protein identification relies on the ability of a technique called tandem mass spectrometry to determine the amino acid sequence for portions of the protein being analyzed. In our lab, this involves the use of electrospray ionization (ESI).
We currently have active projects that cover a broad spectrum of biological systems from plants to animals and humans. These include the identification and determination of function of proteins isolated from corn mitochondria, the role of calcium binding proteins in homeostasis in swine, and characterization of proteins associated with AIDS related dementia and Alzheimer's disease.
Our lab routinely collaborates not only with members of the Chemistry Department but with scientists from across the University of Nebraska system. This includes researchers in the Center for Biotechnology, the Plant Science Initiative, the Nebraska Center for Virology, and the University of Nebraska Medical Center in Omaha.
Cerny Publication
Molecular and Genetic Evidence for a Virus-Encoded Glycosyltransferase Involved in Protein Glycosylation, M.V. Graves, C. T. Bernadt, R.L. Cerny, J.L. Van Etten, Virology, 285, 332-345 (2001).
In Vivo Modifications of the Maize Mitochondrial Small Heat Stress Protein, HSP22 A.A.Lund, D.M. Rhoads, A.L. Lund, R.L. Cerny, T.E Elthon, J. Biol. Chem., 276, 29924-29929(2001).
Reaction mechanism, evolutionary analysis and role of zinc in Drosophila methionine-R-sulfoxide reductase, R.A. Kumar, A. Koc, R.L. Cerny and V.N. Gladyshev, J. Biol. Chem., in press.
