Postdoctoral, University of Nebraska - Lincoln
Ph.D. University of North Carolina
B.S. University of Nebraska
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.
For more information, please visit the Cerny Research Group Homepage.
Quantitative Analysis of Glycation Sites on HSA by 18O-Labelling MALDI-TOF MS. Barnaby, Omar S.; Wa, Chunling; Cerny, Ron; Clarke, William; Hage, David S. Department of Chemistry, University of Nebraska Lincoln, Lincoln, NE, USA. Abstracts, 43rd Midwest Regional Meeting of the American Chemical Society, Kearney, NE, United States, October 8-11 (2008), MWRM-115. Publisher: American Chemical Society, Washington, D. C Conference; Meeting
Phosphorylation of MUC1 by Met modulates interaction with p53 and MMP1 expression. Singh, Pankaj K.; Behrens, Michelle E.; Eggers, John P.; Cerny, Ronald L.; Bailey, Jennifer M.; Shanmugam, Kandavel; Gendler, Sandra J.; Bennett, Eric P.; Hollingsworth, Michael A. Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska, Omaha, NE, USA. Journal of Biological Chemistry (2008), 283(40), 26985-26995. Publisher: American Society for Biochemistry and Molecular Biology
Identification of Guanylate Cyclases and Related Signaling Proteins in Sperm Tail from Sea Stars by Mass Spectrometry. Nakachi, Mia; Matsumoto, Midori; Terry, Philip M.; Cerny, Ronald L.; Moriyama, Hideaki. Department of Biosciences and Informatics, Keio University, Hiyoshi, Kouhoku-ku, kohama, Japan. Marine Biotechnology (2008), 10(5), 564-571. Publisher: Springer