![\"Programme](\"https://www.epfl.ch/campus/art-culture/wp-content/uploads/2026/09/LES_CULTURELLES_1920x1080_programme_complet.png\")
\r\n\r\nThe EPFL EcoCloud Center is proud to invite you to the Annual Event 2026.
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\r\nOnce again we will be welcoming you to Lausanne Palace.
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\r\nThe Event will feature a keynote presentation:\r\n
Wave functions describing bound states of electronic systems satisfy high-dimensional Schrödinger equations whose potentials exhibit Coulomb singularities at particle-collision configurations. These singularities generate cusps that limit the global regularity of the wave function in spectral Barron spaces, which are particularly relevant to the analysis of Fourier-based approximation methods and neural networks.
\r\nIn this talk, we study the effect of extracting a truncated Jastrow factor designed to capture the leading coalescence singularities while preserving the asymptotic behavior of the wave function at infinity. We show that the resulting quotient gains one full order of spectral Barron regularity: whereas the original wave function typically belongs to spaces of order (s<1), the Jastrow quotient belongs to those of order (s<2). An explicit hydrogenic example shows that the threshold (s=2) is natural.
\r\nThe proof relies on conjugating the Hamiltonian by the Jastrow factor and carrying out a global Fourier-space analysis. It combines resolvent estimates, precise control of singular coefficients, and a fixed-point argument separating low and high frequencies.
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\r\nThe electronic structure reading group brings together researchers and students interested in mathematical aspects of electronic structure problems and adjacent topics, including:\r\n
Triple S (Super Sandwich Seminar) will feature three speakers per week, each giving a 15-minute presentation followed by a 5-minute Q&A session.
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\r\nMembers of the university community will be able to take advantage of the health screenings and assessments available at the Health Village, hosted during the first week on the EPFL campus and during the second week on the University of Lausanne campus. They will also have access to information stands run by services and partners committed to promoting a comprehensive, 360-degree approach to health and well-being.
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\r\nThe programme will be available at the end of August on the dedicated website: https://jours-sante.ch/.
SciComm Exchange is a two-day hands-on training program dedicated to science communication and outreach.
\r\nJointly organized by the University of Lausanne (Unil) and the Université Libre de Bruxelles (ULB), it offers early career researchers the opportunity to reflect on their communication and outreach practice, explore a wide variety of formats, engage with experts in the field, and develop their skills in knowledge dissemination.
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\r\nOne research. Dozens of ways to tell its story.
\r\nIt’s up to you to choose which ones you’d like to explore.
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\r\nOn 7 and 8 October 2026, SciComm Exchange invites PhD and postdoctoral researchers from all facultiesto explore new ways of communicating research through hands-on workshops, round-table discussions and meetings with specialists in the field.
\r\nNew for this edition: the Video Hackathon.
\r\nOver two days, a group of participants will be guided by audiovisual professionals to create short videos centered on a key question: why do we communicatescience, and to whom?
\r\nParticipants from previous editions sum up their experience as follows: \r\n
You can apply to participate and find all the relevant information (speakers, abstracts, program,...) on the event website: https://www.cecam.org/workshop-details/g-protein-coupled-receptors-functional-dynamics-revealed-by-experimental-and-computational-structural-data-1488.
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\r\nRegistration is required to attend the full event, take part in the social activities and present a poster at the poster session (if any). However, the EPFL community is welcome to attend specific lectures without registration if the topic is of interest to their research. Do not hesitate to contact the CECAM Event Manager if you have any question.
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\r\nDescription
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\r\nG protein-coupled receptors (GPCRs) represent a vast and diverse class of transmembrane proteins that orchestrate a wide range of physiological processes by responding to both endogenous and exogenous ligands [1,2]. These receptors are essential to critical functions such as metabolism, immune regulation, neuronal signaling, and sensory perception - including vision and olfaction. Due to their physiological relevance and membrane accessibility, GPCRs are the targets of approximately 34% of all prescribed medications, accounting for nearly 27% of the global pharmaceutical market [3].
\r\nDespite their pharmaceutical importance, key aspects of GPCR function remain elusive. The canonical activation model posits that agonist binding to the extracellular orthosteric site triggers allosteric changes - most notably, the outward displacement of transmembrane helices 5 (TM5) and 6 (TM6) on the intracellular side - ultimately leading to receptor activation [2-4]. However, recent evidence suggests a more nuanced mechanism. In several GPCRs, activation appears to involve cooperative engagement between the agonist and the G protein. For example, the G protein may disrupt an \"inactivating ionic lock\" - a salt bridge between TM3 and TM6 - while the agonist stabilizes the active conformation. In some receptors, this is complemented by the formation of an “activating ionic lock” between TM5 and TM6 [5-8]. These dual contributions are considered thermodynamically essential for full activation [7].
\r\nAdding further complexity, GPCR activity is regulated by conformational microswitches and finely tuned intra-protein interaction networks. These dynamic rearrangements are difficult to capture and often elude direct correlation with functional outcomes. Moreover, allosteric ligands - which bind sites distinct from the orthosteric pocket - are being increasingly identified [9-12], along with small molecules capable of biased signaling, i.e., preferential activation of specific intracellular pathways [11-13, 16, 17]. These findings reveal a rich and underexplored conformational landscape that governs GPCR signaling. In addition, native membrane components—such as lipids and interacting proteins, including GPCR oligomers—are known to significantly modulate receptor function [11, 18-22].
\r\nTo disentangle these intricacies, computational modeling has become indispensable, offering atomistic insight into GPCR conformational dynamics and mechanistic understanding [1-2, 7, 11, 14, 16–21, 23]. Nevertheless, key questions remain - particularly regarding the structural basis of biased signaling, strategies for leveraging allosteric networks in pharmacology, and the modulatory role of the lipid environment. Addressing these gaps is crucial for both fundamental biology and the rational design of next-generation GPCR-targeting drugs with improved selectivity and safety profiles.
\r\nThese scientific challenges form the foundation of our upcoming workshop, which will focus on the latest experimental and computational approaches for studying the functional dynamics of GPCRs. Given the profound health, economic, and societal implications of modulating these receptors with precision, we aim to strengthen the interdisciplinary nature of the event by increasing the representation of experimental research and integrating cutting-edge artificial intelligence applications into the program.
\r\nBuilding upon the success of the 2022 and 2024 editions - which led to new collaborations and a landmark publication in Nature Reviews Drug Discovery [24] - our goal is to further enhance communication and collaboration between experimentalists and theoreticians. The workshop will serve as a reference point for young scientists and students, offering a platform to interact with leading international experts. We are confident that this initiative will foster insightful discussions and contribute meaningfully to advancing the field of GPCR pharmacology.
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\r\nReferences
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\r\n[2] P. Conflitti, E. Lyman, M. Sansom, P. Hildebrand, H. Gutiérrez-de-Terán, P. Carloni, T. Ansell, S. Yuan, P. Barth, A. Robinson, C. Tate, D. Gloriam, S. Grzesiek, M. Eddy, S. Prosser, V. Limongelli, Nat. Rev. Drug. Discov., 24, 251-275 (2025)
\r\n[3] L. Picard, A. Orazietti, D. Tran, A. Tucs, S. Hagimoto, Z. Qi, S. Huang, K. Tsuda, A. Kitao, A. Sljoka, R. Prosser, Nat. Chem. Biol., 21, 71-79 (2024)
\r\n[4] B. Huang, C. St. Onge, H. Ma, Y. Zhang, Drug Discovery Today, 26, 189-199 (2021)
\r\n[5] D. Di Marino, P. Conflitti, S. Motta, V. Limongelli, Nat. Commun., 14, 6439 (2023)
\r\n[6] G. Milligan, R. Ward, S. Marsango, Current Opinion in Cell Biology, 57, 40-47 (2019)
\r\n[7] S. Huang, O. Almurad, R. Pejana, Z. Morrison, A. Pandey, L. Picard, M. Nitz, A. Sljoka, R. Prosser, eLife, 11, (2022)
\r\n[8] A. Duncan, W. Song, M. Sansom, Annu. Rev. Pharmacol. Toxicol., 60, 31-50 (2020)
\r\n[9] A. Morales-Pastor, T. Miljuš, M. Dieguez-Eceolaza, T. Stępniewski, V. Ledesma-Martin, F. Heydenreich, T. Flock, B. Plouffe, C. Le Gouill, J. Duchaine, D. Sykes, C. Nicholson, E. Koers, W. Guba, A. Rufer, U. Grether, M. Bouvier, D. Veprintsev, J. Selent, Nat. Commun., 16, 5265 (2025)
\r\n[10] A. Faouzi, H. Wang, S. Zaidi, J. DiBerto, T. Che, Q. Qu, M. Robertson, M. Madasu, A. El Daibani, B. Varga, T. Zhang, C. Ruiz, S. Liu, J. Xu, K. Appourchaux, S. Slocum, S. Eans, M. Cameron, R. Al-Hasani, Y. Pan, B. Roth, J. McLaughlin, G. Skiniotis, V. Katritch, B. Kobilka, S. Majumdar, Nature, 613, 767-774 (2022)
\r\n[11] M. Wall, E. Hill, R. Huckstepp, K. Barkan, G. Deganutti, M. Leuenberger, B. Preti, I. Winfield, S. Carvalho, A. Suchankova, H. Wei, D. Safitri, X. Huang, W. Imlach, C. La Mache, E. Dean, C. Hume, S. Hayward, J. Oliver, F. Zhao, D. Spanswick, C. Reynolds, M. Lochner, G. Ladds, B. Frenguelli, Nat. Commun., 13, 4150 (2022)
\r\n[12] D. Wootten, A. Christopoulos, M. Marti-Solano, M. Babu, P. Sexton, Nat. Rev. Mol. Cell. Biol., 19, 638-653 (2018)
\r\n[13] D. Hilger, M. Masureel, B. Kobilka, Nat. Struct. Mol. Biol., 25, 4-12 (2018)
\r\n[14] D. Aranda-García, T. Stepniewski, M. Torrens-Fontanals, A. García-Recio, M. Lopez-Balastegui, B. Medel-Lacruz, A. Morales-Pastor, A. Peralta-García, M. Dieguez-Eceolaza, D. Sotillo-Nuñez, T. Ding, M. Drabek, C. Jacquemard, J. Jakowiecki, W. Jespers, M. Jiménez-Rosés, V. Jun-Yu-Lim, A. Nicoli, U. Orzel, A. Shahraki, J. Tiemann, V. Ledesma-Martin, F. Nerín-Fonz, S. Suárez-Dou, O. Canal, G. Pándy-Szekeres, J. Mao, D. Gloriam, E. Kellenberger, D. Latek, R. Guixà-González, H. Gutiérrez-de-Terán, I. Tikhonova, P. Hildebrand, M. Filizola, M. Babu, A. Di Pizio, S. Filipek, P. Kolb, A. Cordomi, T. Giorgino, M. Marti-Solano, J. Selent, Nat. Commun., 16, 2020 (2025)
\r\n[15] D. Thal, A. Glukhova, P. Sexton, A. Christopoulos, Nature, 559, 45-53 (2018)
\r\n[16] L. Slosky, M. Caron, L. Barak, Trends in Pharmacological Sciences, 42, 283-299 (2021)
\r\n[17] C. Zhu, X. Lan, Z. Wei, J. Yu, J. Zhang, Acta Pharmaceutica Sinica B, 14, 67-86 (2024)
\r\n[18] V. D’Amore, P. Conflitti, L. Marinelli, V. Limongelli, Chem, 10, 3678-3698 (2024)
\r\n[19] A. Mafi, S. Kim, W. Goddard, Nat. Chem., 15, 1127-1137 (2023)
\r\n[20] H. Batebi, G. Pérez-Hernández, S. Rahman, B. Lan, A. Kamprad, M. Shi, D. Speck, J. Tiemann, R. Guixà-González, F. Reinhardt, P. Stadler, M. Papasergi-Scott, G. Skiniotis, P. Scheerer, B. Kobilka, J. Mathiesen, X. Liu, P. Hildebrand, Nat. Struct. Mol. Biol., 31, 1692-1701 (2024)
\r\n[21] A. Manglik, T. Kim, M. Masureel, C. Altenbach, Z. Yang, D. Hilger, M. Lerch, T. Kobilka, F. Thian, W. Hubbell, R. Prosser, B. Kobilka, Cell, 161, 1101-1111 (2015)
\r\n[22] M. Congreve, C. de Graaf, N. Swain, C. Tate, Cell, 181, 81-91 (2020)
\r\n[23] J. Lorente, A. Sokolov, G. Ferguson, H. Schiöth, A. Hauser, D. Gloriam, Nat. Rev. Drug. Discov., 24, 458-479 (2025)
\r\n[24] M. Lopez‐Balastegui, T. Stepniewski, M. Kogut‐Günthel, A. Di Pizio, M. Rosenkilde, J. Mao, J. Selent, British. J. Pharmacology., 182, 3211-3224 (2024)\r\n
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