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SUMMARY:Protein folding\, misfolding\, disease and cancer\n - Sir Alan Fer
 sht
DTSTART:20150127T200000Z
DTEND:20150127T211500Z
UID:TALK57323@talks.cam.ac.uk
CONTACT:Adam
DESCRIPTION:Sir Alan Fersht is a pioneer of protein engineering\, which he
  developed for the analysis of the structure\, activity and folding of pro
 teins. He founded the method of phi value analysis for studying protein fo
 lding transition states and methods for high resolution analysis of protei
 n folding in the sub-millisecond time-scale. Furthermore\, Sir Alan is dis
 tinguished for his work on enzyme catalysis. For his instrumental work\, h
 e was elected Fellow of the Royal Society in 1983\, and won the Gabor Meda
 l\, the Davy Medal and the Royal Medal. He was appointed Master of Gonvill
 e and Caius College in 2012 and was named as one of the Times 100 leading 
 scientists in the UK in 2014.\n\n\n\nWe have been accustomed for over 50 y
 ears 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 t
 oxic 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.\n\n\n\nEveryone is
  welcome. Free for members\, £2 on the door for non-members. Followed by 
 refreshments (that means smoothies\, cheese and grapes!).
LOCATION:Department of Pharmacology Lecture Theatre\, Tennis Court Road
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