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PRODID:-//SFB 1551 - ECPv6.17.2//NONSGML v1.0//EN
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X-ORIGINAL-URL:https://crc1551.com
X-WR-CALDESC:Events for SFB 1551
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TZID:UTC
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TZOFFSETFROM:+0000
TZOFFSETTO:+0000
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DTSTART:20220101T000000
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BEGIN:VEVENT
DTSTART;TZID=UTC:20250821T103000
DTEND;TZID=UTC:20250821T113000
DTSTAMP:20250812T081607Z
CREATED:20231122T103722Z
LAST-MODIFIED:20250812T081607Z
UID:10000051-1755772200-1755775800@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Prof. Dr. Tanja Weil
DESCRIPTION:Talk announcement for Tanja Weil.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-tanja-weil/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20250724T103000
DTEND;TZID=UTC:20250724T113000
DTSTAMP:20250626T160104Z
CREATED:20250314T135344Z
LAST-MODIFIED:20250626T160104Z
UID:10000095-1753353000-1753356600@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Prof. Dr. Shikha Dhiman
DESCRIPTION:Methods talk by Prof. Dr. Shikha Dhiman\, Chemistry Department\, Johannes Gutenberg University \nHarnessing Competitive Interactions to Regulate Supramolecular Assembly \nAbstract:\nUnderstanding the interplay between supramolecular polymerization and phase separation is key to unraveling the formation of biomolecular assemblies such as protein fibers and membraneless organelles. I will present a minimal synthetic system—comprising a BTA-based monomer\, surfactant\, and water—that mimics biological condensates through a micelle-to-droplet-to-fiber transition. This pathway\, governed by competitive interactions\, is reversible under external stimuli like temperature and guest molecules. Our findings offer a framework for controlling supramolecular order and dynamics\, with implications for synthetic biology and therapeutic design.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-prof-dr-shikha-dhiman/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20250703T103000
DTEND;TZID=UTC:20250703T113000
DTSTAMP:20250626T155809Z
CREATED:20250313T093000Z
LAST-MODIFIED:20250626T155809Z
UID:10000094-1751538600-1751542200@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Dr. Martin Möckel
DESCRIPTION:Methods talk by Dr. Martin Möckel\, Institute of Molecular Biology (IMB) \nIn vitro veritas – an overview on recombinant protein expression\, purification and quality control \nAbstract: \nRecombinant proteins are critical for basic research\, for example to prove molecular mechanisms\, determine protein structure and study the biophysical properties of proteins in a well-defined environment. In this talk I will give you a glimpse on the art of protein production as is done in our core facility. We will start by looking at molecular cloning techniques for expression vector generation\, as well as pros and cons of various expression systems\, with a focus on E. coli and the baculovirus-insect cell system. This will be followed by a more detailed explanation of various chromatography techniques\, before ending the talk with a short overview of possible quality control measurements. \n 
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-dr-martin-mockel/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20250625T143000
DTEND;TZID=UTC:20250625T153000
DTSTAMP:20250624T125913Z
CREATED:20250528T155320Z
LAST-MODIFIED:20250624T125913Z
UID:10000102-1750861800-1750865400@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Dr. Thomas Quail
DESCRIPTION:Talk by Dr.Thomas Quail\, EMBL Heidelberg\, Cell Biology and Biophysics Unit\n \nTitle: Molecular sociology of self-organising genomes \nAbstract: \nProteins organise the genome across multiple length and time scales. How proteins collectively bridge these scales to generate structure execute enzymatic reactions remains an open question. In this talk\, I will discuss our work on dissecting biophysical mechanisms of genome self-organization\, and how these principles are linked to transcription. To tackle these questions\, we use interdisciplinary approaches that combine single molecule biophysics\, reconstitution biology\, and theory. I will describe how protein condensation acts as an organizing principle of genome organization\, generating forces on DNA that then act as active enzymatic scaffolds. \n 
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-dr-thomas-quail/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20250605T103000
DTEND;TZID=UTC:20250605T113000
DTSTAMP:20250528T135508Z
CREATED:20250314T093009Z
LAST-MODIFIED:20250528T135508Z
UID:10000093-1749119400-1749123000@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Dr. Oleksandra Kukharenko
DESCRIPTION:Methods talk by Dr.Olksandra Kukharenko\, Max Planck Institute for Polymer Research \nTitle: Bridging Scales in Molecular Dynamics Simulations with Machine Learning \nAbstract:\nGrasping the behavior of biomolecules across diverse length and time scales is a persistent challenge in molecular biophysics. While atomistic simulations provide detailed molecular insights\, their high computational cost limits their applicability. Coarse-grained models\, on the other hand\, allow access to longer timescales and larger systems but often sacrifice resolution and accuracy. To connect these approaches meaningfully\, it is essential to develop strategies that can bridge the scales and preserve key thermodynamic properties. \nIn this talk\, I will showcase recent advances in leveraging machine learning for the analysis of free energy landscapes. I will demonstrate how tools such as dimensionality reduction and clustering can uncover key collective variables and metastable states from high-dimensional simulation data. Moreover\, I will explore how these learned representations can facilitate the transfer of insights between different modeling resolutions\, enabling seamless integration of coarse-grained and atomistic simulations. Applications to systems with complex multi-body interactions will illustrate the power of this multiscale\, data-driven perspective. \n 
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-dr-oleksandra-kukharenko/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20241212T103000
DTEND;TZID=UTC:20241212T113000
DTSTAMP:20241209T162017Z
CREATED:20241114T171620Z
LAST-MODIFIED:20241209T162017Z
UID:10000082-1733999400-1734003000@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Helle Ulrich
DESCRIPTION:Getting to know the ubiquitin family – analysis & manipulation \nPosttranslational modifications of proteins play essential regulatory roles in cells as they modulate their targets’ interactions\, localization\, and stability. This is achieved either by changing the biophysical properties of the targets or by providing interaction surfaces for dedicated receptors that elicit a biological signal. In this lecture\, I will give a brief overview over the family of ubiquitin-like modifiers\, their biochemical and biological properties\, their enzymatic machinery\, and their signalling functions in the cell. I will also cover established and innovative techniques to analyse and manipulate their activities in cells.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-helle-ulrich/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20241205T103000
DTEND;TZID=UTC:20241205T113000
DTSTAMP:20240912T155211Z
CREATED:20231122T103437Z
LAST-MODIFIED:20240912T155211Z
UID:10000049-1733394600-1733398200@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - René Ketting
DESCRIPTION:Talk announcement for René Ketting.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-rene-ketting/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20240919T103000
DTEND;TZID=UTC:20240919T113000
DTSTAMP:20240912T140451Z
CREATED:20231122T103609Z
LAST-MODIFIED:20240912T140451Z
UID:10000050-1726741800-1726745400@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Dirk Schneider & Nadja Hellmann
DESCRIPTION:Isolating and characterizing proteins for in vitro condensate formation might be problematic! \nHave you ever worked with isolated proteins? Most work in our group involves the isolation of (typically recombinantly produced) proteins plus their biophysical characterization. During this work\, we encountered several problems associated with the insolation of tagged proteins and/or with their biophysical characterization. We have therefore decided to discuss some problems that typically occur but are often ignored “hands on”. We will focus on the isolation of tagged proteins plus their characterization via CD spectroscopy and/or dynamic light scattering. We will use examples from our own research with a condensate-forming protein to highlight some problems and pitfalls.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-dirk-schneider/
LOCATION:Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230914T090000
DTEND;TZID=UTC:20230914T110000
DTSTAMP:20230906T074757Z
CREATED:20230602T104734Z
LAST-MODIFIED:20230906T074757Z
UID:10000018-1694682000-1694689200@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Svenja Morsbach
DESCRIPTION:Talk announcement for Svenja Morsbach
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-svenja-morsbach/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230824T090000
DTEND;TZID=UTC:20230824T110000
DTSTAMP:20230801T125717Z
CREATED:20230626T063436Z
LAST-MODIFIED:20230801T125717Z
UID:10000031-1692867600-1692874800@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Martin Girard
DESCRIPTION:Talk announcement of Martin Girard \n————————————————————————————————————————————————- \n*From lead to cells: digital alchemy\, multicomponent mixtures\, and chemical regulation* \nby Dr. Martin Girard \nMax-Planck-Institute for Polymer Research
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-martin-girard/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=UTC:20230502T100000
DTEND;TZID=UTC:20230502T180000
DTSTAMP:20230512T071014Z
CREATED:20230417T104033Z
LAST-MODIFIED:20230512T071014Z
UID:10000010-1683021600-1683050400@crc1551.com
SUMMARY:SFB 1551 Seminar Series Event - Lin Guo & Rohit Pappu
DESCRIPTION:Professors Lin Guo and Rohit Pappu will visit for a talk on May 2\, 2023. \n\n*Hidden complexities of condensates formed by simple systems* \nAbstract: \nApplication of the physics of associative macromolecules has led to growing recognition that condensates\, even of relatively simple systems\, form via hierarchies of processes governed by sequence-encoded molecular grammars that go beyond LLPS. The talk will present data and results from experiments and simulations that highlight the importance of phase separation coupled to percolation for systems governed by homotypic interactions\, and the relevance of the coupling between microphase and macrophase separation in systems where homotypic and heterotypic interactions work together. Broader implications for complex multicomponent systems will also be discussed. \nby Professor Rohit Pappu \nWashington University in St. Louis \nDepartment of Biomedical Engineering \n  \n*Reversing Aberrant Phase Transitions of ALS-linked Disease Protein: FUS* \nAbstract: \nLiquid-liquid phase separation (LLPS) mediates the formation of diverse membraneless organelles\, such as stress granules (SGs) in the cytoplasm. Despite clear biological utility\, dysregulated liquid-liquid phase separation can be detrimental. For example\, phase-separated stress granules enrich RNA-binding proteins (RBPs)\, such as TDP-43 and FUS\, which have an intrinsic tendency to form fibrils that are closely tied to fatal neurodegenerative disorders\, including amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Therefore\, it is important to understand how cells regulate the liquid-liquid phase separation of biomolecular condensates\, which includes maintaining beneficial phases and simultaneously preventing pathological phase separation and fibrillization. As RNA-binding proteins localize mainly in the nucleus\, the phase separation of FUS and TDP-43 can be regulated by both nuclear import receptors and short RNAs. For example\, we found that phase separation of FUS can be regulated by Karyopherinβ2 (Kapβ2)\, which recognizes the proline/tyrosine–nuclear localization signal (PY-NLS) at the C-terminus of FUS protein. On the other hand\, phase separation of TDP-43 can be regulated by the Importina/Karyopherinb1 complex\, which binds to the canonical NLS of TDP-43. In vivo\, Kapβ2 prevents FUS accumulating in stress granules\, restores nuclear FUS localization and function. By preventing and reversing aberrant FUS phase transition and cytoplasmic localization\, Kapβ2 is able to rescue neurodegeneration caused by disease-linked FUS. Our results indicate that regulating FUS LLPS by nuclear import receptors could be potential therapeutic strategy for ALS/FTD. \nby Professor Lin Guo \nThomas Jefferson University \nDepartment of Biochemistry and Molecular Biology \nLinGuo_RohitPappu_Talk_Announcement_02052023
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
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