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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

Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alphaA-, alphaB- and R120G alphaB-crystallins.
S Meehan, TPJ Knowles, AJ Baldwin, JF Smith, AM Squires, P Clements, TM Treweek, H Ecroyd, GG Tartaglia, M Vendruscolo, CE Macphee, CM Dobson, JA Carver
– Journal of Molecular Biology
(2007)
372,
470
Protein structure determination from NMR chemical shifts.
A Cavalli, X Salvatella, CM Dobson, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2007)
104,
9615
Life on the edge: a link between gene expression levels and aggregation rates of human proteins
GG Tartaglia, S Pechmann, CM Dobson, M Vendruscolo
– Trends in Biochemical Sciences
(2007)
32,
204
Prediction of local structural stabilities of proteins from their amino acid sequences.
GG Tartaglia, A Cavalli, M Vendruscolo
– Structure
(2007)
15,
139
Determination of conformationally heterogeneous states of proteins
M Vendruscolo
– Current opinion in structural biology
(2007)
17,
15
The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins
B Richter, J Gsponer, P Várnai, X Salvatella, M Vendruscolo
– Journal of biomolecular NMR
(2007)
37,
117
Growth with memory
M Marsili, M Vendruscolo
– EPL (Europhysics Letters)
(2007)
37,
505
Hot sandpiles
G Caldarelli, A Maritan, M Vendruscolo
– Europhysics Letters (EPL)
(2007)
35,
481
A PDZ domain recapitulates a unifying mechanism for protein folding
S Gianni, CD Geierhaas, N Calosci, P Jemth, GW Vuister, C Travaglini-Allocatelli, M Vendruscolo, M Brunori
– Proc Natl Acad Sci U S A
(2006)
104,
128
BPPred: A Web‐based computational tool for predicting biophysical parameters of proteins
CD Geierhaas, AA Nickson, K Lindorff-Larsen, J Clarke, M Vendruscolo
– Protein Science
(2006)
16,
125
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk