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VERSION:2.0
PRODID:-//Memento EPFL//
BEGIN:VEVENT
SUMMARY:CECAM Workshop: "Modeling energy-consuming biomolecular processes"
DTSTART:20240122T140000
DTEND:20240125T120000
DTSTAMP:20260414T071552Z
UID:459fcf3da92ba0a7752bdbd724941150007fbfdf1828dcc54caf4a8f
CATEGORIES:Conferences - Seminars
DESCRIPTION:You can find all the relevant information (speakers\, abstract
 s\, program\,...) on the event website: https://www.cecam.org/workshop-de
 tails/1209\n\nDescription:\nWhile historically cellular processes have bee
 n first modeled according to the laws of equilibrium thermodynamics\, the 
 cell is a non-equilibrium environment driven\, and kept alive\, by the con
 sumption of a formidable quantity of energy: each day\, the human body pro
 duces\, and consumes\, an amount of ATP close to its own mass. Understandi
 ng how energy consumption reshapes the energy landscape driving biomolecul
 ar dynamics and interactions\, and possibly gives rise to novel and unexpe
 cted phenomena\, is thus a crucial step for understanding the molecular ba
 sis of life.\nPioneering experimental and theoretical studies have shown t
 hat non-equilibrium physics is strictly required for correctly describing 
 key cellular processes\, including protein translation and DNA replication
 \, whose remarkable fidelity had already been rationalized in the 1970s [1
 ]\, and molecular motors walking on cytoskeletal filaments [2]\, a staple 
 of biophysics in the 1990s and 2000s. More recently\, a plethora of new no
 n-equilibrium biomolecular phenomena have come under the scrutiny of the c
 ommunity. The ability of proteins to fold to their native states\, which a
 re typically assumed to correspond to equilibrium free-energy minima\, is 
 actually controlled in the cell by a host of ATP-driven co- and post-trans
 lational factors\, including molecular chaperones\, that can maintain prot
 eins functional even under adverse conditions [3]. Simple equilibrium poly
 mer models cannot describe the cellular organization of DNA\, which popula
 tes non-equilibrium ensembles controlled by Structural Maintenance of Chro
 mosomes (SMC) proteins by means of their ATP consuming action [4-6]. Many 
 bacterial cells use a complex dance of GTPase molecules that bind to and u
 nbind from membranes to access dynamically unstable states\, inaccessible 
 in any equilibrium description\, that spontaneously mark the position wher
 e cell division has to occur [7]. Membranes are constantly deformed\, pinc
 hed and excised by the concerted action of lipid kinases and phosphatases 
 and by GTP- and ATP- consuming protein machines [8]. Furthermore\, biomole
 cular condensates\, which are currently recognized as key players in cellu
 lar organization\, are intimately regulated by energy-consuming enzymes an
 d may display non-equilibrium\, functional properties [9].\nWhile experime
 nts are providing ever more precise information about these fascinating pr
 ocesses\, a renewed interest and new developments in non-equilibrium stati
 stical physics have provided a new lens for their theoretical modeling. At
  the same time\, efficient computational approaches have to be devised to 
 face the technical challenges associated to the simulation of non-equilibr
 ium cellular processes\, which intimately rely on the interplay between bi
 omolecular dynamics and enzymatic reactions [10-12].\nThe goal of this wor
 kshop is to bring together leading researchers to discuss recent experimen
 tal and theoretical progresses in the field\, to identify key challenges a
 nd to foster further collaborations\, with final aim of pushing the bounda
 ries of current approaches and develop novel tools capable of providing a 
 detailed yet comprehensive picture of non-equilibrium cellular functioning
  at the molecular scale.\n\nRéférences:\n[1] J. Hopfield\, Proc. Natl. A
 cad. Sci. U.S.A.\, 71\, 4135-4139 (1974)\n[2] F. Jülicher\, A. Ajdari\, 
 J. Prost\, Rev. Mod. Phys.\, 69\, 1269-1282 (1997)\n[3] P. Goloubinoff\, 
 A. Sassi\, B. Fauvet\, A. Barducci\, P. De Los Rios\, Nat. Chem. Biol.\, 
 14\, 388-395 (2018)\n[4] J. Marko\, P. De Los Rios\, A. Barducci\, S. Gr
 uber\, Nucleic Acids Research\, 47\, 6956-6972 (2019)\n[5] R. Takaki\, A.
  Dey\, G. Shi\, D. Thirumalai\, Nat. Commun.\, 12\, 5865 (2021)\n[6] M. G
 anji\, I. Shaltiel\, S. Bisht\, E. Kim\, A. Kalichava\, C. Haering\, C. De
 kker\, Science\, 360\, 102-105 (2018)\n[7] F. Brauns\, G. Pawlik\, J. Hal
 atek\, J. Kerssemakers\, E. Frey\, C. Dekker\, Nat. Commun.\, 12\, 3312 (
 2021)\n[8] B. Antonny\, C. Burd\, P. De Camilli\, E. Chen\, O. Daumke\, K.
  Faelber\, M. Ford\, V. Frolov\, A. Frost\, J. Hinshaw\, T. Kirchhausen\, 
 M. Kozlov\, M. Lenz\, H. Low\, H. McMahon\, C. Merrifield\, T. Pollard\, P
 . Robinson\, A. Roux\, S. Schmid\, EMBO. J.\, 35\, 2270-2284 (2016)\n[9] 
 M. Hondele\, S. Heinrich\, P. De Los Rios\, K. Weis\, Emerging Topics in L
 ife Sciences\, 4\, 343-354 (2020)\n[10] K. Popov\, J. Komianos\, G. Papoi
 an\, PLoS. Comput. Biol.\, 12\, e1004877 (2016)\n[11] S. Assenza\, A. Sas
 si\, R. Kellner\, B. Schuler\, P. De Los Rios\, A. Barducci\, eLife\, 8\,
  (2019)\n[12] M. Foglino\, E. Locatelli\, C. Brackley\, D. Michieletto\, C
 . Likos\, D. Marenduzzo\, Soft Matter\, 15\, 5995-6005 (2019)
LOCATION:BCH 2103 https://plan.epfl.ch/?room==BCH%202103
STATUS:CONFIRMED
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