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

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
Nature communications
(2016)
7
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
Microfluidic Diffusion Viscometer for Rapid Analysis of Complex Solutions
P Arosio, K Hu, FA Aprile, T Müller, TPJ Knowles
Analytical Chemistry
(2016)
88
An Environmentally Sensitive Fluorescent Dye as a Multidimensional Probe of Amyloid Formation
EV Yates, G Meisl, TPJ Knowles, CM Dobson
J Phys Chem B
(2016)
120
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 Combinatorial Science
(2016)
18
Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.
WM Jacobs, TPJ Knowles, D Frenkel
PLoS computational biology
(2016)
12
Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation
E van Dijk, P Varilly, TPJ Knowles, D Frenkel, S Abeln
Physical review letters
(2016)
116
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
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, SIA Cohen, MBD Müller, S Linse, EAA Nollen, CM Dobson, TPJ Knowles, M Vendruscolo
Sci Adv
(2016)
2
Oligomers of heat-shock proteins: Structures that don't imply function
WM Jacobs, TPJ Knowles, D Frenkel
(2016)

Co-Director

Research Interest Groups

Telephone number

01223 336344

Email address