Mass spectrometry and structure, dynamics and function of the small heat shock proteins

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• Justin Benesch
• Wednesday 05 December 2007, 10:30-11:30
• Unilever Lecture Theatre, Unilever Centre, Department of Chemistry.

If you have a question about this talk, please contact Giorgio Favrin.

The sHSPs are a virtually ubiquitous family of molecular chaperones which act to prevent protein deposition in the cell. Despite this, and their implication in a number of disease states, these proteins remain poorly understood. What is clear, however, is that these proteins exhibit remarkable structural and dynamical variability that are likely to be integral to their chaperone function. Here I will present data obtained from mass spectrometry approaches which we have developed to probe aspects of eukaryotic sHSPs. We categorize the stunning polydispersity and concomitant 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.

This talk is part of the Biophysics Colloquia - (Chemistry) series.

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