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Tuomas Knowles

Probing proteins in small volumes

The self-assembly of protein molecules into functional structures underlies core aspects of biological activity in living systems. When this process doesn't occur correctly, however, misfolded and misassembled species are formed, which can have deleterious activity, including compromising the viability of neurons and thus leading to neurodegeneration in the context of Alzheimer's and Parkinson's diseases. This talk outlines our efforts to develop and apply new physical chemistry approaches to probe and understand protein self-assembly and misassembly, and their roles in biological function and malfunction. A particular focus will be on probing protein behaviour using microfluidic tools, and I will discuss a number of cases where experiments in ultra-small volumes allow key aspects of protein behaviour to be quantified that remain challenging to obtain from conventional bulk experiments.

 

 

Tuomas Knowles

Tuomas Knowles

Department of Chemistry and Cavendish Laboratory

University of Cambridge

Tuomas Knowles studied Biology at the University of Geneva, and Physics at ETH Zurich, where he graduated in 2004. He moved to Cambridge in 2004 as a graduate student working in the Cavendish Laboratory and the Nanoscience Centre. In 2008 he was elected to a Research Fellowship at St John's College, Cambridge, and was then appointed to a University Lectureship in Physical Chemistry in 2010, joining the faculty at the Department of Chemistry in Cambridge. He then successively held a University Readership between 2013 and 2015 and a Professorship since 2015 in the Department of Chemistry. Since 2016 he is Professor of Physical Chemistry and Biophysics in the Department of Chemistry and at the Cavendish Laboratory, and is co-director of the Cambridge Centre for Protein Misfolding Diseases in Cambridge. He is the recipient of a number of prizes including the Royal Society of Chemistry Corday-Morgan Prize and the Raymond and Beverly Sackler International Prize in Biophysics.

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