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CATEGORIES:Biophysics Colloquia - (Chemistry)
SUMMARY:Mass spectrometry and structure\, dynamics and fun
 ction of the small heat shock proteins - Justin Be
 nesch
DTSTART;TZID=Europe/London:20071205T103000
DTEND;TZID=Europe/London:20071205T113000
UID:TALK9336AThttp://talks.cam.ac.uk
URL:http://talks.cam.ac.uk/talk/index/9336
DESCRIPTION:The sHSPs are a virtually ubiquitous family of mol
 ecular chaperones which act to prevent protein dep
 osition in the cell. Despite this\, and their impl
 ication in a number of disease states\, these prot
 eins remain poorly understood. What is clear\, how
 ever\, is that these proteins exhibit remarkable s
 tructural and dynamical variability that are likel
 y to be integral to their chaperone function. Here
  I will present data obtained from mass spectromet
 ry approaches which we have developed to probe asp
 ects of eukaryotic sHSPs. We categorize the stunni
 ng polydispersity and concomitant structural heter
 ogeneity of the alpha-crystallins\, the most well-
 know of the mammalian sHSPs\, and together with re
 al-time monitoring of their dynamics and substrate
  binding advance a new view of the function of the
 se most interesting of chaperones.
LOCATION:Unilever Lecture Theatre\, Unilever Centre\, Depar
 tment of Chemistry
CONTACT:Giorgio Favrin
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