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Yusuf Hamied Department of Chemistry

 

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

Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity
J Dworzak, B Renvoisé, J Habchi, EV Yates, C Combadière, TP Knowles, CM Dobson, C Blackstone, O Paulsen, PM Murphy
– PloS one
(2015)
10,
e0127730
Aggregation-prone amyloid-β·CuII 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)
16,
1293
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
– Chem Sci
(2015)
6,
4215
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)
6,
7025
Preventing peptide and protein misbehavior.
P Arosio, G Meisl, M Andreasen, TPJ Knowles
– Proc Natl Acad Sci U S A
(2015)
112,
5267
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
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
– Proceedings of the National Academy of Sciences
(2015)
112,
e1994
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)
22,
207
The physical basis of protein misfolding disorders
TPJ Knowles, M Vendruscolo, CM Dobson
– Physics Today
(2015)
68,
36
A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers.
SIA Cohen, P Arosio, J Presto, FR Kurudenkandy, H Biverstal, L Dolfe, C Dunning, X Yang, B Frohm, M Vendruscolo, J Johansson, CM Dobson, A Fisahn, TPJ Knowles, S Linse
– Nat Struct Mol Biol
(2015)
22,
207
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Research Interest Groups

Telephone number

01223 336344

Email address

tpjk2@cam.ac.uk