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TZID:Europe/Paris
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BEGIN:VEVENT
UID:1-500@lptms.universite-paris-saclay.fr
DTSTART:20170419T110000Z
DTEND:20170419T120000Z
DTSTAMP:20170403T081707Z
URL:http://www.lptms.universite-paris-saclay.fr/seminars/physics-biology-i
 nterface-seminar-alessandro-barducci/
SUMMARY:Physics-Biology interface seminar: Alessandro Barducci - LPTMS\, sa
 lle 201\, 2ème étage\, Bât 100\, Campus d'Orsay - 19 Avr 17 11:00
DESCRIPTION:Molecular chaperones as cellular non-equilibrium machines. \nAl
 essandro Barducci (Centre de Biochimie Structurale-INSERM\, Montpellier)\n
 \nMolecular chaperones are a  vast class of proteins that maintain protein
  homeostasis in the cell and are thus essential for cell viability. In ord
 er to assist protein folding and prevent misfolding\, most chaperones proc
 eed through conformational cycles that are regulated by complex interactio
 n networks and fueled by ATP-hydrolysis. A remarkable example are the 70-k
 Dalton heat shock proteins (Hsp70s)\, which are essential in prokaryotes a
 nd eukaryotes and are involved in co-translational folding\, refolding of 
 misfolded and aggregated proteins\, protein translocation\, and protein de
 gradation. While the investigation of Hsp70 cycle has attracted great atte
 ntion in the last decades\, the actual role of ATP-hydrolysis and\, thus o
 f energy consumption\, in the chaperone function has been long unaddressed
 . Here we will prove how biochemical data\, recent single-molecule fluores
 cence experiments and molecular simulations can be combined into an approp
 riate theoretical framework to show that: i) ATP hydrolysis allows Hsp70 c
 haperones to increase their affinity for the client proteins beyond the bo
 unds imposed by equilibrium thermodynamics ii) This ultra-affinity can be 
 exploited to perform mechanical work on client proteins thus avoiding the 
 formation of misfolded and potentially cytotoxic species. \n
CATEGORIES:physbio,seminars
LOCATION:LPTMS\, salle 201\, 2ème étage\, Bât 100\, Campus d'Orsay\, 15 
 Rue Georges Clemenceau\, Orsay\, 91405\, France
GEO:48.698185;2.181768
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  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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