Assistant Research Professor (Teschke laboratory)
University of Connecticut
Department of Molecular & Cell Biology
91 North Eagleville Road, Unit 3125
Biology/Physics Building 206
Storrs, CT 06269-3125
Education: BS University of Delhi, MS University of Delhi, PhD Wesleyan University, Postdoc, University of Connecticut
Research Interests: The main goal of Teschke lab is focused on understanding the folding of viral proteins. Using bacteriophage P22 as a model system, we are trying to study how the viral proteins assemble with high fidelity into complex structures that form viruses. My project is to investigate the assembly of the portal protein complex during the procapsid assembly of bacteriophage P22.
1. R. K. Lokareddy, R. S. Sankhala, A. Roy, P. V. Afonine, T. Motwani, C. M. Teschke, K. N. Parent, G. Cingolani, Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation. Nature communications 8, 14310 (2017).
2. D. Z. Keifer, T. Motwani, C. M. Teschke, M. F. Jarrold, Measurement of the accurate mass of a 50 MDa infectious virus. Rapid communications in mass spectrometry : RCM 30, 1957-1962 (2016).
3. D. Z. Keifer, T. Motwani, C. M. Teschke, M. F. Jarrold, Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry. Journal of the American Society for Mass Spectrometry 27, 1028-1036 (2016).
4. W. Wu, J. C. Leavitt, N. Cheng, E. B. Gilcrease, T. Motwani, C. M. Teschke, S. R. Casjens, A. C. Steven, Localization of the Houdinisome (Ejection Proteins) inside the Bacteriophage P22 Virion by Bubblegram Imaging. mBio 7, (2016).
5. C. Harprecht, O. Okifo, K. J. Robbins, T. Motwani, A. T. Alexandrescu, C. M. Teschke, Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain. The Journal of biological chemistry 291, 11359-11372 (2016).
6. J. R. Cortines, T. Motwani, A. A. Vyas, C. M. Teschke, Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein. Journal of virology 88, 5287-5297 (2014).