(Not accepting graduate students)
University of Nebraska-Lincoln
710 Hamilton Hall
Lincoln, NE 68588-0304
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.
(1) Overexpression of human fatty acid transport protein 2/very long chain acyl-CoA synthetase 1 (FATP2/Acsvl1) reveals distinct patterns of trafficking of exogenous fatty acids By: Melton, Elaina M.; Cerny, Ronald L.; DiRusso, Concetta C.; et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS Volume:440 Issue: 4 Pages: 743-748 Published: NOV 1 2013
(2) Development of Affinity Microcolumns for Drug-Protein Binding Studies in Personalized Medicine: Interactions of Sulfonylurea Drugs with in vivo Glycated Human Serum Albumin By: Anguizola, Jeanethe; Joseph, K. S.; Barnaby, Omar S.; et al. ANALYTICAL CHEMISTRY Volume: 85 Issue: 9 Pages: 4453-4460 Published: MAY 7 2013
(3) Molecular recognition of sulfotyrosine and phosphotyrosine by the Src homology 2 domain By: Ju, Tong; Niu, Wei; Cerny, Ronald; et al. MOLECULAR BIOSYSTEMS Volume: 9 Issue: 7 Pages: 1829-1832 Published: 2013