skip to content

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

Small-world view of the amino acids that play a key role in protein folding
M Vendruscolo, NV Dokholyan, E Paci, M Karplus
– Phys Rev E Stat Nonlin Soft Matter Phys
(2002)
65,
061910
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 Genetics
(2002)
47,
379
Statistical properties of contact vectors.
A Kabakçioglu, I Kanter, M Vendruscolo, E Domany
– Phys Rev E Stat Nonlin Soft Matter Phys
(2002)
65,
041904
Automated assignment of SCOP and CATH protein structure classifications from FSSP scores.
G Getz, M Vendruscolo, D Sachs, E Domany
– Proteins Structure Function and Genetics
(2002)
46,
405
Energetics of enzyme stability
M Vendruscolo
– Trends Biotechnol
(2002)
20,
1
Protein Folding Using Inter-Residue Contacts
M Vendruscolo
– FIRST INTERNATIONAL SYMPOSIUM ON 3D DATA PROCESSING VISUALIZATION AND TRANSMISSION
(2002)
83,
1
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
– Journal of biological physics
(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
(2001)
44,
133
  • <
  • 76 of 80
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk