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Protein folding, misfolding, disease and cancer

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Sir Alan Fersht is a pioneer of protein engineering, which he developed for the analysis of the structure, activity and folding of proteins. He founded the method of phi value analysis for studying protein folding transition states and methods for high resolution analysis of protein folding in the sub-millisecond time-scale. Furthermore, Sir Alan is distinguished for his work on enzyme catalysis. For his instrumental work, he was elected Fellow of the Royal Society in 1983, and won the Gabor Medal, the Davy Medal and the Royal Medal. He was appointed Master of Gonville and Caius College in 2012 and was named as one of the Times 100 leading scientists in the UK in 2014.

We have been accustomed for over 50 years of thinking of proteins as beautifully folded structures. But we now know that many proteins are disordered in both the test tube and the cell, and that many others unfold or misfold to lose their activity or cause toxic aggregates. Such misfolding can lead to diseases such as Alzheimer’s or even cancer. Sir Alan will use the tumour suppressor p53 as a paradigm to represent those facets of protein structure, their importance and how his group is designing new drugs to stabilise proteins.

Everyone is welcome. Free for members, £2 on the door for non-members. Followed by refreshments (that means smoothies, cheese and grapes!).

This talk is part of the SciSoc – Cambridge University Scientific Society series.

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