Proteins Behaving Badly? Aggregation, disease and nanotechnology, Professor Athene Donald FRS January 22, 2008

To attend this event please email [email protected].

Protein aggregation turns up in many guises, some beneficial but many not. The public at large are familiar with many of the diseases, such as vCJD and Alzheimers, in which protein aggregation into so-called amyloid fibrils is implicated. Thus protein aggregation has a bad name. However, structures essentially identical in outline but formed from very different proteins can also be seen as benign or even beneficial: the texture of yoghurt and cheese, for instance, is also related to the ability of milk proteins to aggregate. And, finally, it has been suggested that protein fibrils could also be used to make nanowires of interest to nanotechnologists.

This talk will look at the way in which proteins can aggregate under different circumstances, concentrating on generic behaviour rather than specific details of the different proteins. The similarities between the behaviour of different proteins can be used to provide an indicator of the underlying mechanisms which govern aggregation.

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