Mehmet Kesimer

     Research Assistant Professor

       Mailing address:

     University of North Carolina at Chapel Hill

     Department of Biochemistry and Biophysics

     Chapel Hill, NC 27599-7248

        Office: CF Center, 4021 Thurston Bowles Bldg.

        Phone: (919) 843 2577

        Email : kesimer@med.unc.edu

Research Interests:

My biochemical work is centered upon the characterization of the large mucin gene products (Mr 2-3 million) and the complexes they make (Mr 10-100 million) essential for the formation of the mucus gels vital for epithelial protection and function. My current work is focussed around the human lung where there are many hypersecretory human diseases including asthma, cystic fibrosis, and chronic bronchitis in which these glycoconjugates are centrally implicated. We are using a well defined human cell culture system (NHTBE) that mimics human airway epithelia to identify proteins, large glycoconjugates and mucins by using a shutgun proteomics approach. We have identified 5 different Mucins (MUC 5B, AC, MUC1, MUC4 and MUC16) and more than 100 proteins in the NHTBE cell secretion. I am also interested in the proteins that interact with these mucins. We found that some of these proteins are probably in covalent complexes with the mucins as they can only be released by reduction of disulphide bonds. Our studies are broad ranging and seek to build up a picture of the biophysics and chemistry of these complex phenotypes, the network of their interactions that constitutes a mucosal surface and the mechanisms of their biosynthesis, assembly and secretion.

My main proteomics interest includes designing and implementing novel mass spectral methods for identifying proteins and glycoproteins in mucus gels where conventional proteomic methods do not work. Many of the molecules are heavily modified and thus MS methods for characterising post-translational modifications are vital in this work. We are using state-of-the-art mass spectrometer systems such as MALDI-TOF and 1D, 2D and even 3D separations  employing nano-LC-MS-MS.

Our laboratory (Sheehan Lab.) is established with a wide range of state of the art biochemical, chemical and physical methods including MALDI-TOF and ESI-MS-MS mass spectrometry, electron and atomic force microscopy, hydrodynamics, theoretical molecular dynamics and a variety of surface physics tools.

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Last Updated09/30/2009 08:36:40 PM