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Professor Tuomas Knowles

Portrait of tpjk2

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.

Selected publications

An analytical solution to the kinetics of breakable filament assembly, Science, 326, 1533 (2009)

Role of intermolecular forces in defining material properties of protein nanofibrils, Science 318, 1900 (2007)


Analysis of the length distribution of amyloid fibrils by centrifugal sedimentation.
P Arosio, T Cedervall, TP Knowles, S Linse – Analytical biochemistry (2016)
Microfluidic Diffusion Viscometer for Rapid Analysis of Complex Solutions.
P Arosio, K Hu, FA Aprile, T Müller, TP Knowles – Anal Chem (2016) 88, 3488
A Fragment-Based Method of Creating Small-Molecule Libraries to Target the Aggregation of Intrinsically Disordered Proteins
P Joshi, S Chia, J Habchi, TP Knowles, CM Dobson, M Vendruscolo – ACS Comb Sci (2016) 18, 144
Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation.
E van Dijk, P Varilly, TP Knowles, D Frenkel, S Abeln – Phys Rev Lett (2016) 116, 078101
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, TP Knowles, D Klenerman – Proceedings of the National Academy of Sciences of the United States of America (2016) 113, E1206
An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation.
EV Yates, G Meisl, TP Knowles, CM Dobson – J Phys Chem B (2016) 120, 2087
Automated Ex Situ Assays of Amyloid Formation on a Microfluidic Platform.
KL Saar, EV Yates, T Müller, S Saunier, CM Dobson, TP Knowles – Biophys J (2016) 110, 555
An anticancer drug suppresses the primary nucleation reaction that initiates the production of the toxic Aβ42 aggregates linked with Alzheimer's disease.
J Habchi, P Arosio, M Perni, AR Costa, M Yagi-Utsumi, P Joshi, S Chia, SI Cohen, MB Müller, S Linse, EA Nollen, CM Dobson, TP Knowles, M Vendruscolo – Sci Adv (2016) 2, e1501244
Molecular mechanisms of protein aggregation from global fitting of kinetic models.
G Meisl, JB Kirkegaard, P Arosio, TC Michaels, M Vendruscolo, CM Dobson, S Linse, TP Knowles – Nature protocols (2016) 11, 252
Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.
WM Jacobs, TP Knowles, D Frenkel – PLoS computational biology (2016) 12, e1004756
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Research Group

Research Interest Groups

Telephone number

01223 763845 (shared)
01223 336344

Email address