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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

Growth with memory
M Marsili, M Vendruscolo
– Europhysics Letters
(2007)
37,
505
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
– Proceedings of the National Academy of Sciences of the United States of America
(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
Geometry, energetics, and dynamics of hydrogen bonds in proteins: Structural information derived from NMR scalar couplings
J Gsponer, H Hopearuoho, A Cavalli, CM Dobson, M Vendruscolo
– J Am Chem Soc
(2006)
128,
15127
Dynamic visions of enzymatic reactions
M Vendruscolo, CM Dobson
– Science
(2006)
313,
1586
Characterization of the residual structure in the unfolded state of the Delta131Delta fragment of staphylococcal nuclease.
CJ Francis, K Lindorff-Larsen, RB Best, M Vendruscolo
– Proteins
(2006)
65,
145
Relation between native ensembles and experimental structures of proteins.
RB Best, K Lindorff-Larsen, MA DePristo, M Vendruscolo
– Proceedings of the National Academy of Sciences
(2006)
103,
10901
Relation between native ensembles and experimental structures of proteins
RB Best, K Lindorff-Larsen, MA DePristo, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2006)
103,
10901
A protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank
U Bastolla, M Porto, HE Roman, M Vendruscolo
– BMC Evol Biol
(2006)
6,
43
Structural Comparison of the Two Alternative Transition States for Folding of TI I27
CD Geierhaas, RB Best, E Paci, M Vendruscolo, J Clarke
– Biophys J
(2006)
91,
263
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk