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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

An algorithm and experimental protocol to obtain the kinetic parameters of fibrillar growth from a first-principles general model of breakable filament assembly
SI Cohen, M Sandal, L Rajah, CM Dobson, M Vendruscolo, TPJ Knowles
– FEBS JOURNAL
(2010)
277,
257
Intrinsic determinants of neurotoxic aggregate formation by the amyloid β peptide
A-C Brorsson, B Bolognesi, GG Tartaglia, SL Shammas, G Favrin, I Watson, DA Lomas, F Chiti, M Vendruscolo, CM Dobson, DC Crowther, LM Luheshi
– Biophysical Journal
(2010)
98,
1677
Physicochemical determinants of chaperone requirements.
GG Tartaglia, CM Dobson, FU Hartl, M Vendruscolo
– J Mol Biol
(2010)
400,
579
Time averaging of NMR chemical shifts in the MLF peptide in the solid state
I De Gortari, G Portella, X Salvatella, VS Bajaj, PCA van der Wel, JR Yates, MD Segall, CJ Pickard, MC Payne, M Vendruscolo
– J Am Chem Soc
(2010)
132,
5993
Effects of disease-associated mutations on the aggregation process of the 93-residue N-terminal fragment of human apolipoprotein A-I
S Raimondi, F Guglielmi, S Giorgetti, S Di Gaetano, A Arciello, A Relini, SM Doglia, A Natalello, P Pucci, P Mangione, L Obici, G Merlini, M Stoppini, GG Tartaglia, M Vendruscolo, R Piccoli, V Bellotti
– AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
(2010)
17,
39
Networks in Cell Biology
M Buchanan, G Caldarelli, P De Los Rios, F Rao, M Vendruscolo
(2010)
i
Network views of the cell
P De Los Rios, M Vendruscolo
(2010)
4
An analytical solution to the kinetics of breakable filament assembly.
TPJ Knowles, CA Waudby, GL Devlin, SIA Cohen, A Aguzzi, M Vendruscolo, EM Terentjev, ME Welland, CM Dobson
– Science
(2009)
326,
1533
Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements.
JR Allison, P Varnai, CM Dobson, M Vendruscolo
– Journal of the American Chemical Society
(2009)
131,
18314
Analysis of Sub-τ c and Supra-τ c Motions in Protein Gβ1 Using Molecular Dynamics Simulations
JM Bui, J Gsponer, M Vendruscolo, CM Dobson
– Biophysical journal
(2009)
97,
2513
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk