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DTSTART;TZID=UTC:20260122T103000
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SUMMARY:SFB 1551 Seminar Series Event - Dr. Davide Mercadante
DESCRIPTION:“Functional advantages of protein structural disorder as revealed by integrative biophysics” \nDr. Davide Mercadante (School of Chemical Sciences\, The University of Auckland\, Auckland\, New Zealand) \nSummary:\nSince the discovery that protein structural disorder holds functional relevance intrinsically disordered proteins (IDPs) have become a cornerstone of biophysics.\nCharacterized by extremely high dynamics\, IDPs are elusive by nature and traditional structural biology techniques remain largely uncapable of providing an exhaustive understanding of their behavior.\nHowever\, the qualitative and quantitative integration of computational experimental techniques well-versed to assess protein dynamics\, thus provides a powerful framework to elucidate IDPs’ dynamics-driven functions. This talk will overview how the integration of biophysical approaches within the experimental and computational realms has favored the discovery of new functional paradigms empowered by protein disorder. 1–5 I will showcase how simulations employing all-atom or coarse-grained modelling of protein chains\, can help linking the conformational behavior of IDPs to their ensemble-based function: and how it can be possible to obtain experimentally sound protein ensembles from coarse grained protein models\, through a direct integration of NMR observables into simulations. 6\,7 \nReferences\n1. Milles\, S. et al. Plasticity of an Ultrafast Interaction between Nucleoporins and Nuclear Transport Receptors. Cell 163\, 734–745 (2015).\n2. Swain\, B. C. et al. Disordered regions of human eIF4B orchestrate a dynamic self-association landscape. Nat Commun 15\, 8766 (2024).\n3. Heidarsson\, P. O. et al. Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein. Nat Chem 14\, 224–231 (2022).\n4. Bjarnason\, S. et al. DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2. Nat Commun 15\, (2024).\n5. Buholzer\, K. J. et al. Multilayered allosteric modulation of coupled folding and binding by phosphorylation\, peptidyl-prolyl cis / trans isomerization\, and diversity of interaction partners. Journal of Chemical Physics 157\, (2022).\n6. Cullen\, M. et al. Integrating NMR restraints into coarse-grained simulations: toward accurate conformational ensembles of complex protein systems. bioRxiv 2025.12.22.695971 (2025) doi:10.64898/2025.12.22.695971.\n7. Cullen\, M. et al. Capturing secondary structure in coarse grained intrinsically disordered proteins with simulations driven by chemical shifts. bioRxiv 2026.01.06.697719 (2026) doi:10.64898/2026.01.06.697719.
URL:https://crc1551.com/our-event/sfb-1551-seminar-series-event-dr-davide-mercadante/
LOCATION:Biocenter I\, EG 00.187\, Hanns-Dieter-Hüsch-Weg 15\, Mainz
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DTSTART;VALUE=DATE:20260128
DTEND;VALUE=DATE:20260131
DTSTAMP:20251216T115027Z
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SUMMARY:SFB1551 Winter School 2026
DESCRIPTION:Content is protected.
URL:https://crc1551.com/our-event/sfb1551-winter-school-2026/
LOCATION:Basecamp Bonn\, In d. Raste 1\, Bonn\, 53129\, Germany
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