Single-molecule FRET (smFRET) has become a very standard tool to probe protein dynamics. The time-resolution in smFRET is fundamentally related to the fluorescence intensity of the probe attached to the protein of interest. By employing plasmonic-based nanosctructures, e.g., zero-mode waveguide, we aim to enhance the photon output of the fluorescent probes and thereby increasing the time-resolution in smFRET. This would allow us to probe protein dynamics which still eludes us.
To avoid photodamage under high-light, plants have evolved feedback-controlled machinery to dissipate the excess energy as heat. The collective mechanism of dissipating the excess light energy is known as non-photochemical quenching (NPQ). I investigate the mechanism of NPQ using single-molecule spectroscopy and model membranes. A detailed understanding of the NPQ mechanism will help us to enhance the crop yield.
Directed evolution is a powerful technique to alter the protein functions for their industrial, research and therapeutic applications via genetic diversity and selections thereafter. I employ microfluidic-based multi-parametric high-throughput sorter for directed evolution of the photophysical properties of red fluorescent proteins. The resulting proteins have higher brightness that enhances their utility as fluorescent markers in live-cell imaging.
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