Education
PhD, Clemson University, 2022
Lab information
Located within Rice University’s Shared Equipment Authority (SEA), this advanced biophysics and bioimaging facility provides high-precision instrumentation for studying single-molecule interactions, surface kinetics, and 3D cellular dynamics. The lab features a Lumicks C-Trap Optical Tweezer system for simultaneous force measurement and fluorescence microscopy, a QSense Omni Quartz Crystal Microbalance with Dissipation (QCM-D) for tracking nanoscale mass deposition and viscoelastic properties in real time, and a Zeiss Light Sheet 7 microscope for gentle, low-phototoxicity 3D imaging of live organisms and cleared tissues. Together, these platforms enable researchers across biophysics, soft matter physics, bioengineering, and bioscience to perform high-resolution molecular manipulation, quantitative surface analysis, and fast volumetric bioimaging.
https://research.rice.edu/sea/instruments/microscopes/microscope-lumicks-optical-tweezer
Publications
https://scholar.google.co.in/citations?hl=en&user=jj9KgLkAAAAJ&view_op=list_works&authuser=1SERS hotspots for sensing applications (2024, Under preparation)
• Godar, S., Oristian, J., Hinsch, V., Wentworth, K., Lopez, E., Enverso, G. and Alper, J. Light chain 2 is a Tctex-type related axonemal dynein light chain that regulates directional ciliary motility in T. brucei. PLoS Pathogen (2022) (Publication funded under the Open Access Funding Initiative Award, 2022)
• Pabbathi, A., Coleman, L., Godar, S., Paul, A., Garlapati, A., Spencer, M., Eller, J. and Alper, J., Long-Range Electrostatic Interactions Significantly Modulate the Affinity of Dynein for Microtubules. Biophysical Journal (2021)
• Ma, J.*, Saikia, N.*, Godar, S.*, Hamilton, G., Alper, J., Ding, F. and Sanabria, H., Ensemble switching unveils a kinetic rheostat mechanism of the eukaryotic thiamine pyrophosphate riboswitch. RNA (2021), * Equally contributing authors
• Li, L., Jia, Z., Peng, Y., Godar, S., Getov, I., Teng, S., Alper, J. and Alexov, E. Forces and Disease: Electrostatic force differences caused by mutations in kinesin motor domains can distinguish between disease-causing and non-disease-causing mutations. Scientific Reports (2017).