Dr. Zhang from the University of Illinois has invented a generalizable optogenetic system for post-translational knock-in of a target protein, GLIMPSe. GLIMPSe offers...
Dr. Zhang from the University of Illinois has invented a generalizable optogenetic system for post-translational knock-in of a target protein, GLIMPSe. GLIMPSe offers bidirectional control over post-translational protein activity with high spatiotemporal resolution. GLIMPSe works by fusing the target protein with a protease recognition site (tevS), a photosensitive caging molecule (eLOV), and three degradation sequences. GLIMPSe also involves connecting TEV protease with LEXY, a light-sensitive nuclear export signal molecule.
When there is no light exposure, degradation sequences tag the target protein for degradation. When there is light exposure, the nuclear export signal on LEXY is exposed, allowing TES to be exported from the nucleus. Also, upon exposure to light, tevS is exposed by eLOV, allowing TEV to cleave the degradation sequence from the complex, stabilizing the target protein.
Primary Application: Optogenetic neuroscience research
Benefit: Provides bi-directional control of protein dynamics with high spatiotemporal resolution
Dr. Zhang from the University of Illinois has invented a generalizable optogenetic system for post-translational knock-in of a target protein, GLIMPSe. GLIMPSe offers...
Dr. Zhang from the University of Illinois has invented a generalizable optogenetic system for post-translational knock-in of a target protein, GLIMPSe. GLIMPSe offers bidirectional control over post-translational protein activity with high spatiotemporal resolution. GLIMPSe works by fusing the target protein with a protease recognition site (tevS), a photosensitive caging molecule (eLOV), and three degradation sequences. GLIMPSe also involves connecting TEV protease with LEXY, a light-sensitive nuclear export signal molecule.
When there is no light exposure, degradation sequences tag the target protein for degradation. When there is light exposure, the nuclear export signal on LEXY is exposed, allowing TES to be exported from the nucleus. Also, upon exposure to light, tevS is exposed by eLOV, allowing TEV to cleave the degradation sequence from the complex, stabilizing the target protein.
Primary Application: Optogenetic neuroscience research
Benefit: Provides bi-directional control of protein dynamics with high spatiotemporal resolution
Professor Dahmen and collaborators have developed a method for determining failure stress and other mechanical properties of materials using a conventional nanoindentation...
Professor Dahmen and collaborators have developed a method for determining failure stress and other mechanical properties of materials using a conventional nanoindentation instrument. This method relies on a model previously developed by Prof. Dahmen's group which assumes solid materials contain elastically coupled weak spots that can slip in response to an applied load. These slips can be seen as jumps in nanoindenter displacement which can be further characterized to determine failure stress and other mechanical properties. Using this model, the high throughput screening of the relative brittleness of materials can be accomplished in as little as 10 measurements in an effectively non-destructive fashion. Additionally, this versatile method can be applied to amorphous and crystalline solids, such as bulk metallic glasses, high entropy alloys, and a large number of other solids.
