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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

Introduction to the special issue of GENE
M Porto, HE Roman, M Vendruscolo
– Gene
(2008)
422,
vii
Mutational Analysis of the Aggregation-Prone and Disaggregation-Prone Regions of Acylphosphatase
M Calamai, GG Tartaglia, M Vendruscolo, F Chiti, CM Dobson
– Journal of molecular biology
(2008)
387,
965
Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation.
G Calloni, C Lendel, S Campioni, S Giannini, A Gliozzi, A Relini, M Vendruscolo, CM Dobson, X Salvatella, F Chiti
– J Am Chem Soc
(2008)
130,
13040
Towards quantitative predictions in cell biology using chemical properties of proteins
M Vendruscolo, GG Tartaglia
– Mol Biosyst
(2008)
4,
1170
Prediction by Graph Theoretic Measures of Structural Effects in Proteins Arising from Non-Synonymous Single Nucleotide Polymorphisms
TMK Cheng, Y-E Lu, M Vendruscolo, P Lio', TL Blundell
– PLoS computational biology
(2008)
4,
e1000135
Characterizing the first steps of amyloid formation for the ccbeta peptide.
B Strodel, AW Fitzpatrick, M Vendruscolo, CM Dobson, DJ Wales
– The Journal of Physical Chemistry B
(2008)
112,
9998-10004
Mapping of two networks of residues that exhibit structural and dynamical changes upon binding in a PDZ domain protein.
A Dhulesia, J Gsponer, M Vendruscolo
– Journal of the American Chemical Society
(2008)
130,
8931
A stochastic method for the reconstruction of protein structures from one-dimensional structural profiles
K Wolff, M Vendruscolo, M Porto
– Gene
(2008)
422,
47
The Zyggregator method for predicting protein aggregation propensities.
GG Tartaglia, M Vendruscolo
– Chemical Society Reviews
(2008)
37,
1395
Prediction of aggregation-prone regions in structured proteins.
GG Tartaglia, AP Pawar, S Campioni, CM Dobson, F Chiti, M Vendruscolo
– Journal of Molecular Biology
(2008)
380,
425
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk