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Dr 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)

Publications

Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry
XM Zhou, U Shimanovich, TW Herling, S Wu, CM Dobson, TP Knowles, S Perrett – ACS Nano (2015) 9, 5772
Aggregation-Prone Amyloid-β⋅Cu II Species Formed on the Millisecond Timescale under Mildly Acidic Conditions
JT Pedersen, CB Borg, TC Michaels, TP Knowles, P Faller, K Teilum, L Hemmingsen – Chembiochem (2015) 16, 1293
Preventing peptide and protein misbehavior.
P Arosio, G Meisl, M Andreasen, TP Knowles – Proceedings of the National Academy of Sciences of the United States of America (2015) 112, 5267
A microfluidic platform for quantitative measurements of effective protein charges and single ion binding in solution.
TW Herling, P Arosio, T Müller, S Linse, TP Knowles – Physical chemistry chemical physics : PCCP (2015) 17, 12161
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, TP Knowles, C Alfonso, G Rivas, AY Abramov, JM Valpuesta, CM Dobson, N Cremades – Proceedings of the National Academy of Sciences of the United States of America (2015) 112, E1994
The physical basis of protein misfolding disorders
TPJ Knowles, M Vendruscolo, CM Dobson – Physics Today (2015) 68, 36
On the lag phase in amyloid fibril formation
P Arosio, TP Knowles, S Linse – Physical chemistry chemical physics : PCCP (2015) 17, 7606
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers
SI 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, TP Knowles, S Linse – Nature Structural & Molecular Biology (2015) 22, 207
Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation.
C Galvagnion, AK Buell, G Meisl, TC Michaels, M Vendruscolo, TP Knowles, CM Dobson – Nature Chemical Biology (2015) 11, 229
Kinetic theory of protein filament growth: Self-consistent methods and perturbative techniques
TCT Michaels, TPJ Knowles – International Journal of Modern Physics B (2015) 29, 1530002
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Research Group

Research Interest Groups

Telephone number

01223 336344
01223 763845 (shared)

Email address

tpjk2@cam.ac.uk