2009 Press Releases

Eminent Scientist to deliver British Biophysical Society Lecture
05.11.2009

Professor Helen Saibil, FRS, Bernal Professor of Structural Biology at Birkbeck College and Institute for Structural Molecular Biology, University of London, will deliver the Biophysical Society Lecture at UCC on Wednesday next, November 11th at 1pm in Room LG51, Cavanagh Building. The lecture is titled “Cryo Electron Microscopy of Chaperone Machines”. 
The British Biophysical Society promotes use of physical methods to answer fundamental biological problems and to this end sponsors an annual lecture tour to allow an eminent scientist present the Biophysical Society Lecture in UCC, UCD and Queen’s University Belfast on successive days. Professor David Sheehan (Biochemistry Dept), a member of the British Biophysical Society Committee, organises this tour.

All are welcome to attend!

Background and context: Proteins of complex organisms are generally larger and more complex than those of bacteria and often need help to fold correctly. This is achieved by complexes of stress-response proteins called chaperonins providing a protected folding chamber. We now know that many important diseases (e.g. Alzheimer’s) have a protein mis-folding component and understanding the role of protein folding in disease is now a major research frontier. Prof Saibil works on structure-function relationships in molecular chaperones and the process of protein misfolding into amyloid fibrils (http://people.cryst.bbk.ac.uk/~ubcg16z/). Her interests are in analyzing shape changes in macromolecular machines, cryo-electron microscopy and image processing. Her work on the Escherichia coli chaperonin has elucidated the detailed mechanism of this complex protein folding machine. Another major interest is in studies of the conformational changes in membrane pore formation by bacterial toxins and in immune defence. Prof Saibil is a member of EMBO and was elected as a Fellow of the Royal Society in 2006 and of the Academy of Medical Sciences in 2009.

Image: Chaperonin complex with a newly folded substrate protein encapsulated in the folding chamber (Clare et al., Nature 2009, 457; 107-111)

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