BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//wp-events-plugin.com//6.4.7.2//EN
TZID:Europe/Paris
X-WR-TIMEZONE:Europe/Paris
BEGIN:VEVENT
UID:1-504@lptms.universite-paris-saclay.fr
DTSTART:20170531T110000Z
DTEND:20170531T120000Z
DTSTAMP:20170320T145957Z
URL:http://www.lptms.universite-paris-saclay.fr/seminars/physics-biology-i
 nterface-seminar-thierry-bizebard/
SUMMARY:Physics-Biology interface seminar: Thierry Bizebard - LPTMS\, salle
  201\, 2ème étage\, Bât 100\, Campus d'Orsay - 31 Mai 17 11:00
DESCRIPTION:Ribosome assembly studied by single-molecule force measurements
 \nThierry Bizebard (IBPC\, Paris)\nRibosomes belong to the most complicate
 d structures in biology. Their assembly is a question of fundamental inter
 est\, but is still poorly understood. In vitro reconstitution studies have
  shown that the ribosome assembly process is highly cooperative and starts
  with the binding of a few ribosomal (r-) proteins to rRNA\, but how these
  early binders act is unknown. Our work focuses on the initial phase of th
 e assembly of the large subunit (50S) of the E. coli ribosome\, which invo
 lves 23S rRNA\, five r-proteins and a selection of assembly “helper” p
 roteins.\nOur force measurements on single RNA molecules have allowed us t
 o pinpoint several important properties of the early-binding r-proteins we
  have studied:\n- These proteins bind with high cooperativity to the rRNA 
 (as would be expected to obtain a high yield of fully assembled and active
  ribosomes).\n- The r-proteins act as molecular clamps\, stabilising the R
 NA 3D structure.\n- As such\, they afford a strong mechanical and energeti
 cal stabilisation of the ribonucleoprotein structure (which is also probab
 ly necessary for optimum activity).\nIn the near future\, we intend to fur
 ther improve the potential of our single-molecule measurements by implemen
 ting combined force/fluorescence manipulations\, and apply this methodolog
 y to our study of the early phase of E. coli large ribosomal subunit assem
 bly.\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
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
END:VEVENT
END:VCALENDAR