Professor Tuomas Knowles | Page 51 | Yusuf Hamied Department of Chemistry

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Professor of Physical Chemistry and Biophysics

1920 Professor of Physical Chemistry

Our research

We study the physical and chemical aspects of the behaviour of biopolymers and other soft systems. Much of our work has been focused on the physical aspects underlying the self-assembly of protein molecules. Self-organisation is the driving force generating complex matter in nature, and the process by which the machinery providing functionality in living systems is assembled. The goal of our research is to understand the physical and chemical factors which control the structures and dynamics of biomolecular assemblies, and the connections between the nanoscale characteristics of the component molecules and the physical properties of large-scale assemblies and their behaviour on a mesoscopic to macroscopic scale. The techniques used in our laboratory include biosensors, optical lithography, microfluidic devices and scanning probe microscopy and spectroscopy. We work both with natural and synthetic polymers and our interests range from fundamental chemical physics to technological applications in material science and molecular medicine.

Watch Professor Knowles discuss his research

Take a tour of the Sir Rodney Sweetnam laboratory

Publications

The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model.

V Kakkar, C Månsson, EP de Mattos, S Bergink, M van der Zwaag, MAWH van Waarde, NJ Kloosterhuis, R Melki, RTP van Cruchten, S Al-Karadaghi, P Arosio, CM Dobson, TPJ Knowles, GP Bates, JM van Deursen, S Linse, B van de Sluis, C Emanuelsson, HH Kampinga

– Mol Cell

(2016)

62,

272

(doi: 10.1016/j.molcel.2016.03.017)

A general reaction network unifies the aggregation behaviour of the A$\beta$42 peptide and its variants

G Meisl, X Yang, CM Dobson, S Linse, TPJ Knowles

(2016)

(doi: 10.48550/arxiv.1604.00828)

Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation.

P Arosio, T Cedervall, TPJ Knowles, S Linse

– Analytical biochemistry

(2016)

504,

7

(doi: 10.1016/j.ab.2016.03.015)

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.

P Arosio, TCT Michaels, S Linse, C Månsson, C Emanuelsson, J Presto, J Johansson, M Vendruscolo, CM Dobson, TPJ Knowles

– Nat Commun

(2016)

7,

10948

(doi: 10.1038/ncomms10948)

Quantitative thermophoretic study of disease-related protein aggregates

M Wolff, JJ Mittag, TW Herling, ED Genst, CM Dobson, TPJ Knowles, D Braun, AK Buell

– Scientific reports

(2016)

6,

22829

(doi: 10.1038/srep22829)

Microfluidic Diffusion Viscometer for Rapid Analysis of Complex Solutions

P Arosio, K Hu, FA Aprile, T Müller, TPJ Knowles

– Analytical chemistry

(2016)

88,

3488

(doi: 10.1021/acs.analchem.5b02930)

An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation

EV Yates, G Meisl, TPJ Knowles, CM Dobson

– The journal of physical chemistry. B

(2016)

120,

2087

(doi: 10.1021/acs.jpcb.5b09663)

A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins.

P Joshi, S Chia, J Habchi, TPJ Knowles, CM Dobson, M Vendruscolo

– ACS Comb Sci

(2016)

18,

144

(doi: 10.1021/acscombsci.5b00129)

Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.

WM Jacobs, TPJ Knowles, D Frenkel

– PLoS Comput Biol

(2016)

12,

e1004756

(doi: 10.1371/journal.pcbi.1004756)

Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.

M Iljina, GA Garcia, MH Horrocks, L Tosatto, ML Choi, KA Ganzinger, AY Abramov, S Gandhi, NW Wood, N Cremades, CM Dobson, TPJ Knowles, D Klenerman

– Proceedings of the National Academy of Sciences of the United States of America

(2016)

113,

e1206

(doi: 10.1073/pnas.1524128113)