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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

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
(2001)
44,
79
Three key residues form a critical contact network in a protein folding transition state
M Vendruscolo, E Paci, CM Dobson, M Karplus
– Nature
(2001)
409,
641
Comparison of two optimization methods to derive energy parameters for protein folding: Perceptron and Z score
M Vendruscolo, LA Mirny, EI Shakhnovich, E Domany
– Proteins: Structure, Function, and Genetics
(2000)
41,
192
Toward an energy function for the contact map representation of proteins
K Park, M Vendruscolo, E Domany
– Proteins Structure Function and Bioinformatics
(2000)
40,
237
Structurally constrained protein evolution: Results from a lattice simulation
U Bastolla, M Vendruscolo, HE Roman
– The European Physical Journal B
(2000)
15,
385
A statistical mechanical method to optimize energy functions for protein folding.
U Bastolla, M Vendruscolo, EW Knapp
– Proc Natl Acad Sci U S A
(2000)
97,
3977
Can a pairwise contact potential stabilize native protein folds against decoys obtained by threading?
M Vendruscolo, R Najmanovich, E Domany
– Proteins
(2000)
38,
134
Folding Lennard‐Jones proteins by a contact potential
C Clementi, M Vendruscolo, A Maritan, E Domany
– Proteins: Structure, Function, and Genetics
(2000)
37,
544
Comparison of two optimization methods to derive energy parameters for protein folding: Perceptron and Z score
M Vendruscolo, LA Mirny, EI Shakhnovich, E Domany
– Proteins
(2000)
41,
192
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk