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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

Statistical properties of contact vectors
A Kabakçioglu, I Kanter, M Vendruscolo, E Domany
– Physical review. E, Statistical, nonlinear, and soft matter physics
(2002)
65,
041904
Native and non-native interactions along protein folding and unfolding pathways.
E Paci, M Vendruscolo, M Karplus
– Proteins Structure Function and Bioinformatics
(2002)
47,
379
Statistical properties of contact vectors
A Kabakçioglu, I Kanter, M Vendruscolo, E Domany
– Physical Review E Statistical Physics Plasmas Fluids and Related Interdisciplinary Topics
(2002)
65,
7
Automated assignment of SCOP and CATH protein structure classifications from FSSP scores.
G Getz, M Vendruscolo, D Sachs, E Domany
– Proteins
(2002)
46,
405
Energetics of enzyme stability
M Vendruscolo
– Trends in biotechnology
(2002)
20,
1
Protein Folding Using Inter-Residue Contacts
M Vendruscolo
– FIRST INTERNATIONAL SYMPOSIUM ON 3D DATA PROCESSING VISUALIZATION AND TRANSMISSION
(2002)
83,
724
Assessment of the Quality of Energy Functions for Protein Folding by Using a Criterion Derived With the Help of the Noisy Go Model
M Vendruscolo
– J Biol Phys
(2001)
27,
205
Connectivity of neutral networks and structural conservation in protein evolution
U Bastolla, M Porto, HE Roman, M Vendruscolo
– J. Mol. Evol.
(2001)
56,
243
Generalized comparative modeling (GENECOMP): A combination of sequence comparison, threading, and lattice modeling for protein structure prediction and refinement
A Kolinski, MR Betancourt, D Kihara, P Rotkiewicz, J Skolnick
– Proteins Structure Function and Bioinformatics
(2001)
44,
133
How to guarantee optimal stability for most representative structures in the Protein Data Bank.
U Bastolla, J Farwer, EW Knapp, M Vendruscolo
– Proteins: Structure, Function, and Bioinformatics
(2001)
44,
79
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk