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SUMMARY:Mass spectrometry and structure\, dynamics and function of the sma
 ll heat shock proteins - Justin Benesch
DTSTART:20071205T103000Z
DTEND:20071205T113000Z
UID:TALK9336@talks.cam.ac.uk
CONTACT:Giorgio Favrin
DESCRIPTION:The sHSPs are a virtually ubiquitous family of molecular chape
 rones which act to prevent protein deposition in the cell. Despite this\, 
 and their implication in a number of disease states\, these proteins remai
 n poorly understood. What is clear\, however\, is that these proteins exhi
 bit remarkable structural and dynamical variability that are likely to be 
 integral to their chaperone function. Here I will present data obtained fr
 om mass spectrometry approaches which we have developed to probe aspects o
 f eukaryotic sHSPs. We categorize the stunning polydispersity and concomit
 ant structural heterogeneity of the alpha-crystallins\, the most well-know
  of the mammalian sHSPs\, and together with real-time monitoring of their 
 dynamics and substrate binding advance a new view of the function of these
  most interesting of chaperones.
LOCATION:Unilever Lecture Theatre\, Unilever Centre\, Department of Chemis
 try
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