Research
Proteins and protein complexes have provided researchers for many years with some of nature’s most interesting puzzles, and gaining a more complete understanding of each is undoubtedly one of the most important keys to unlocking the secrets of life. I have always been fascinated with how these proteins function within membranes, performing a range of tasks including transport, signaling, membrane disruption, etc. Currently, our lab is developing and using new microscopy techniques, such as Single-Point Edge Excitation Sub-Diffraction (SPEED) microscopy, combined with a 2D-to-3D transformation algorithm that allows for the conversion of super-resolution images into three-dimensional models. When imaging a rotationally symmetric protein complex in the cell, it is possible to take a two-dimensional super-resolution image, and rotate that image plane 360 degrees to produce a three-dimensional model of the complex; this is the principle behind the algorithm.
Nuclear Pore Complexes (NPCs) are a major focal point of the research in my lab, as a result of both the rotational symmetry of the complex, as well as the high-value that understanding the NPC provides to researchers. Right now, my project is focused on gaining a better understanding of how pre-ribosomal subunits are exported from the nucleus. Using FRET microscopy, we are hoping to elucidate whether or not there is a major conformational change in the pre-ribosomal subunits in order to pass through the NPC, as a result of the relatively large size of the subunits. In an effort to increase the visibility of the fluorescent light emitted from the FRET proteins, we will be employing improved variations of the SPEED microscopy technique. In the future, I am hoping to explore the possibility of expanding the techniques to allow for the analysis of near-rotationally symmetric complexes in the cell, as well as to use the improved microscopy techniques to try and effectively detect auto-fluorescent signals.
