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DTSTART;TZID=UTC:20250605T103000
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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
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DTSTART;TZID=UTC:20250610T113000
DTEND;TZID=UTC:20250610T123000
DTSTAMP:20250606T092307Z
CREATED:20241007T100516Z
LAST-MODIFIED:20250606T092307Z
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SUMMARY:SFB 1551 Seminar Series Event - Prof. Dr. Tuomas Knowles
DESCRIPTION:Protein phase transitions in health\, disease\, and new materials\nBy Prof. Dr. Tuomas Knowles\nUniversity of Cambridge\, UK · Department of Physical Chemistry and Biophysics \nThis talk describes our efforts to measure\, quantify\, understand and modulate at the molecular level the processes that govern protein phase separation and aggregation. We bring together theory\, computation and experiments to discover the molecular mechanisms of aggregation and phase separation. I will discuss how controlling transitions between such phases can help us ameliorate biological malfunction when it occurs in disease\, and well as develop new classes of functional materials.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-prof-dr-tuomas-knowles/
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DTSTART;VALUE=DATE:20250616
DTEND;VALUE=DATE:20250619
DTSTAMP:20250115T102256Z
CREATED:20240807T131158Z
LAST-MODIFIED:20250115T102256Z
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SUMMARY:SFB1551 & SPP2191 Coworker Basecamp
DESCRIPTION:Content is protected.
URL:https://crc1551.com/our-event/sfb1551-spp2191-coworker-basecamp/
LOCATION:Basecamp Bonn\, In d. Raste 1\, Bonn\, 53129\, Germany
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DTSTART;TZID=UTC:20250625T143000
DTEND;TZID=UTC:20250625T153000
DTSTAMP:20250624T125913Z
CREATED:20250528T155320Z
LAST-MODIFIED:20250624T125913Z
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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
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