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Yusuf Hamied Department of Chemistry

 

Professor of Biophysics

Our research

In the last 15 years our research has been focused on the development of methods of characterising the structure, dynamics and interactions of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from nuclear magnetic resonance spectroscopy, as structural restraints in molecular dynamics simulations. Through this approach it is possible to obtain information about a variety of protein conformations, as for example those populated during the folding process, and about protein interactions in complex environments, including those generating aggregate species that are associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases.

Application to neurodegenerative diseases

More recently, these studies have led us to investigate the physico-chemical principles of proteins homeostasis and their application to the development of therapeutic strategies against neurodegenerative diseases. Starting from the observation that proteins are expressed in the cell at levels close to their solubility limits, we are developing approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.

Watch Professor Vendruscolo discuss his research

Take a tour of the Una Finlay Laboratory in the Centre for Misfolding Diseases

Publications

Molecular mechanisms of protein aggregation from global fitting of kinetic models.
G Meisl, JB Kirkegaard, P Arosio, TCT Michaels, M Vendruscolo, CM Dobson, S Linse, TPJ Knowles
– Nature Protocols
(2016)
11,
252
Determination of statistical ensembles of intrinsically disordered proteins using NMR measurements
M Vendruscolo
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2016)
252,
Characterizing the free energy landscape of intrinsically disordered proteins by metadynamics simulation and experiments
D Granata, G Zerze, J Mittal, M Vendruscolo, A Laio
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2016)
252,
Metainference: A Bayesian inference method for heterogeneous systems
M Bonomi, C Camilloni, A Cavalli, M Vendruscolo
– Science advances
(2016)
2,
e1501177
Structural Insights into the Calcium-Mediated Allosteric Transition in the C-Terminal Domain of Calmodulin from Nuclear Magnetic Resonance Measurements.
P Kukic, P Lundström, C Camilloni, J Evenäs, M Akke, M Vendruscolo
– Biochemistry
(2015)
55,
19
Microfluidic diffusion analysis of the sizes and interactions of proteins under native solution conditions
P Arosio, T Müller, L Rajah, EV Yates, FA Aprile, Y Zhang, SIA Cohen, DA White, TW Herling, EJ De Genst, S Linse, M Vendruscolo, CM Dobson, TPJ Knowles
– ACS Nano
(2015)
10,
333
Using Pseudocontact Shifts and Residual Dipolar Couplings as Exact NMR Restraints for the Determination of Protein Structural Ensembles
C Camilloni, M Vendruscolo
– Biochemistry
(2015)
54,
7470
Parmbsc1: A refined force field for DNA simulations
I Ivani, PD Dans, A Noy, A Pérez, I Faustino, A Hospital, J Walther, P Andrio, R Goñi, A Balaceanu, G Portella, F Battistini, JL Gelpí, C González, M Vendruscolo, CA Laughton, SA Harris, DA Case, M Orozco
– Nature Methods
(2015)
13,
55
Structure-Free Validation of Residual Dipolar Coupling and Paramagnetic Relaxation Enhancement Measurements of Disordered Proteins.
FN Newby, A De Simone, M Yagi-Utsumi, X Salvatella, CM Dobson, M Vendruscolo
– Biochemistry
(2015)
54,
6876
ALS/FTD Mutation-Induced Phase Transition of FUS Liquid Droplets and Reversible Hydrogels into Irreversible Hydrogels Impairs RNP Granule Function
T Murakami, S Qamar, JQ Lin, GSK Schierle, E Rees, A Miyashita, AR Costa, RB Dodd, FTS Chan, CH Michel, D Kronenberg-Versteeg, Y Li, S-P Yang, Y Wakutani, W Meadows, RR Ferry, L Dong, GG Tartaglia, G Favrin, W-L Lin, DW Dickson, M Zhen, D Ron, G Schmitt-Ulms, PE Fraser, NA Shneider, C Holt, M Vendruscolo, CF Kaminski, P St George-Hyslop
– Neuron
(2015)
88,
678
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk