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TZID:Europe/Paris
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BEGIN:VEVENT
UID:0-537@lptms.universite-paris-saclay.fr
DTSTART:20180116T110000Z
DTEND:20180116T120000Z
DTSTAMP:20180108T093044Z
URL:https://www.lptms.universite-paris-saclay.fr/seminars/seminaire-du-lpt
 ms-remy-dubertrand-3/
SUMMARY:Séminaire du LPTMS: Rémy Dubertrand &amp\; Pierre Illien - LPTMS\
 , salle 201\, 2ème étage\, Bât 100\, Campus d'Orsay - 16 Jan 18 11:00
DESCRIPTION:A semiclassical perspective to study quantum interacting partic
 les\nRémy Dubertrand (Université de Liège\, Belgique)\nQuantum chaos ha
 ve had a great success to describe various types of one-particle quantum s
 ystems in the semiclassical regime (e.g. large quantum numbers). I will de
 scribe how these techniques can be used to describe quantum systems of int
 eracting particles. For example I contributed to look at Bose Hubbard mode
 l and justify why the spectral statistics agrees with RMT for a certain re
 gime of the ratio between onsite interaction and hopping energies. I will 
 discuss in a more general framework how fruitful a semiclassical approach 
 can be to study such systems of interacting particles.\n\n\n\nEffect of cr
 owding and hydrodynamic interactions on the dynamics of fluctuating system
 s\nPierre Illien (EC2M laboratory\, ESPCI Paris)\nDescribing the interacti
 ons of a fluctuating object with its environment is an ubiquitous problem
  of statistical physics. I will first focus on the dynamics of a driven p
 article in a host medium which hinders its motion through crowding interac
 tions. Going beyond the usual effective descriptions of the environment of
  the active tracer\, we propose a lattice model which takes explicitly int
 o account the correlations between the dynamics of the tracer and the resp
 onse of the bath and for which we determine analytically exact and approxi
 mate solutions\, that reveal intrinsically nonlinear and nonequilibrium pr
 operties.\n\nI will then present recent results that reveal how the diffus
 ivity of enzymes can be enhanced when they are catalytically active. In o
 rder to identify the physical mechanisms at stake in this phenomenon\, we 
 perform measurements on the endothermic and relatively slow enzyme aldolas
 e. We propose a new physical paradigm\, which reveals that the diffusion c
 oefficient of a model enzyme hydrodynamically coupled to its environment i
 ncreases significantly when undergoing changes in conformational fluctuati
 ons in a substrate concentration dependent manner\, and is independent of 
 the overall turnover rate of the underlying enzymatic reaction.
CATEGORIES:seminars
LOCATION:LPTMS\, salle 201\, 2ème étage\, Bât 100\, Campus d'Orsay\, 15 
 Rue Georges Clemenceau\, Orsay\, 91405\, France
GEO:48.698185;2.181768
X-APPLE-STRUCTURED-LOCATION;VALUE=URI;X-ADDRESS=15 Rue Georges Clemenceau\,
  Orsay\, 91405\, France;X-APPLE-RADIUS=100;X-TITLE=LPTMS\, salle 201\, 2è
 me étage\, Bât 100\, Campus d'Orsay:geo:48.698185,2.181768
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