Professor Tuomas Knowles

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

Aggregation-Prone Amyloid-Cu^II Species Formed on the Millisecond Timescale under Mildly Acidic Conditions

JT Pedersen, CB Borg, TCT Michaels, TPJ Knowles, P Faller, K Teilum, L Hemmingsen

Chembiochem

(2015)

1293

(doi: 10.1002/cbic.201500080)

The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation

R Cukalevski, X Yang, G Meisl, U Weininger, K Bernfur, B Frohm, TPJ Knowles, S Linse

Chemical Science

(2015)

4215

(doi: 10.1039/c4sc02517b)

A mechanistic model of tau amyloid aggregation based on direct observation of oligomers.

SL Shammas, GA Garcia, S Kumar, M Kjaergaard, MH Horrocks, N Shivji, E Mandelkow, TPJ Knowles, E Mandelkow, D Klenerman

Nature communications

(2015)

7025

(doi: 10.1038/ncomms8025)

Preventing peptide and protein misbehavior.

P Arosio, G Meisl, M Andreasen, TPJ Knowles

Proc Natl Acad Sci U S A

(2015)

112

5267

(doi: 10.1073/pnas.1505170112)

Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.

SW Chen, S Drakulic, E Deas, M Ouberai, FA Aprile, R Arranz, S Ness, C Roodveldt, T Guilliams, EJ De-Genst, D Klenerman, NW Wood, TPJ Knowles, C Alfonso, G Rivas, AY Abramov, JM Valpuesta, CM Dobson, N Cremades

Proc Natl Acad Sci U S A

(2015)

112

e1994

(doi: 10.1073/pnas.1421204112)

Structural characterization of toxic oligomers that are kinetically trapped during alpha-synuclein fibril formation

SW Chen, S Drakulic, E Deas, MM Ouberai, FA Aprile, R Arranz, S Ness, C Roodveldt, T Guilliams, GE De, D Klenerman, NW Wood, TPJ Knowles, C Alfonso, G Rivas, AY Abramov, JM Valpuesta, CM Dobson, N Cremades

Proceedings of the National Academy of Sciences

(2015)

112

E1994

(doi: 10.1073/pnas.1421204112.)

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.

SIA Cohen, P Arosio, J Presto, FR Kurudenkandy, H Biverstål, L Dolfe, C Dunning, X Yang, B Frohm, M Vendruscolo, J Johansson, CM Dobson, A Fisahn, TPJ Knowles, S Linse

Nature Structural and Molecular Biology

(2015)

207

(doi: 10.1038/nsmb.2971)