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X-WR-CALNAME:GRK 2905 - Ultrafast Nanoscopy
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X-WR-CALDESC:Events for GRK 2905 - Ultrafast Nanoscopy
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DTSTART:20241027T010000
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DTSTART;TZID=Europe/Berlin:20241108T150000
DTEND;TZID=Europe/Berlin:20241108T160000
DTSTAMP:20260428T131157
CREATED:20241106T094030Z
LAST-MODIFIED:20241108T134915Z
UID:1471-1731078000-1731081600@grk2905.de
SUMMARY:Colloquium: Photopharmacology Across Time and Space: Molecular Insights via X-ray Free Electron Lasers
DESCRIPTION:RUN auditorium \n\n\n\nDr. Jörg Standfuss  \n\n\n\nLab. for Biomolecular Research\, PSI Center for Life Sciences\, Switzerland \n\n\n\nStructural biology has been critical for our understanding of how proteins work on the molecular level. However\, resolving the temporal evolution of biological macromolecules in response to activating stimuli—such as the binding of small molecular ligands or drug molecules—remains a challenge. In recent years\, our research group has leveraged X-ray Free Electron Laser facilities to experimentally investigate how retinal-binding rhodopsins\, acting as pumps\, channels\, or light sensors\, are activated at the atomic level across a wide range of time scales. \n\n\n\n\n\n\n\n\n\nf \n\n\n\n\nSee announcement\n\n\n\n\n\n\nIn our latest experiments at the Swiss X-ray Free Electron Laser\, we explored how photoactive azobenzene compounds\, mimicking retinal\, can be used to trigger protein dynamics for structural studies. My presentation will focus on the dissociation dynamics of the photopharmacological drug candidate azo-combretastatin A4 from tubulin\, capturing events from the initial photochemical reaction in the femtosecond range\, through the disruption of high-affinity protein-ligand interactions in nanoseconds\, adaptation of the binding pocket in microseconds\, and the eventual release of the compound in milliseconds. I will discuss the relevance of these findings for our understanding of how anti-cancer drugs destabilize the microtubule network. Furthermore\, I will propose the use of azobenzene-based photoswitches to trigger G protein-coupled receptors and other pharmacologically relevant targets in time-resolved structural biology experiments.
URL:https://grk2905.de/event/colloquium-photopharmacology-across-time-and-space-molecular-insights-via-x-ray-free-electron-lasers/
CATEGORIES:Colloquium
ATTACH;FMTTYPE=image/jpeg:https://grk2905.de/wp-content/uploads/2024/09/Jorg-Standfuss-e1730886513313.jpg
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DTSTART;TZID=Europe/Berlin:20241115T140000
DTEND;TZID=Europe/Berlin:20241115T150000
DTSTAMP:20260428T131157
CREATED:20241001T133813Z
LAST-MODIFIED:20260326T162953Z
UID:1420-1731679200-1731682800@grk2905.de
SUMMARY:RTG Colloquium: Complexity with a purpose: Long range collective vibrations steering protein conformational change
DESCRIPTION:14:00 h \n\n\n\n\n\n\n\n\n\n\n\nRUN auditorium \n\n\n\nProf. Dr. Andrea Markelz \n\n\n\nUniversity at Buffalo College of Arts and Sciences \n\n\n\n\n\n\n\nThe evolutionary advantage of the large-scale structure of proteins surrounding the biochemically active site is not readily apparent. It has been speculated that the structural dynamics provide long-range control of access to the active site. Through anisotropic terahertz micro-spectroscopy (ATM) measurements we find that the photo initiation of orange carotenoid protein’s (OCP) photocycle is accompanied with switching in the protein structural vibrations\, before long range structural change can occur. The ATM spectral changes are reversible and calculations reproduce the changes in ATM spectra\, with features red shifted from the measurements. Averaging the vibrational displacement autocorrelation matrix over the spectrally relevant region and thermally occupied starting configurations finds changes in the correlations for residues 80-113 with residues 151-164\, and for residues 280-291 with residues 265-275. These regions are those previously predicted to be involved in the structural modification necessary for a critical step in the photocycle. The results provide the first evidence that structural vibrational change can actuate conformational change for function.
URL:https://grk2905.de/event/grk-colloquium-prof-dr-andrea-markelz/
CATEGORIES:Colloquium
ATTACH;FMTTYPE=image/jpeg:https://grk2905.de/wp-content/uploads/2024/10/Markelz-scaled-e1727789922881.jpg
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