skip to content
Home

Yusuf Hamied Department of Chemistry

 

Professor Michele Vendruscolo

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

Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations.
MM Dedmon, K Lindorff-Larsen, J Christodoulou, M Vendruscolo, CM Dobson
– J Am Chem Soc
(2004)
127,
476
(doi: 10.1021/ja044834j)
Prediction of site-specific amino acid distributions and limits of divergent evolutionary changes in protein sequences
M Porto, HE Roman, M Vendruscolo, U Bastolla
– Mol Biol Evol
(2004)
22,
630
(doi: 10.1093/molbev/msi048)
Prinicipal eigenvector of contact matrices and hydrophobicity profiles in proteins
U Bastolla, M Porto, HE Roman, M Vendruscolo
– Proteins: Structure, Function, and Bioinformatics
(2004)
58,
22
(doi: 10.1002/prot.20240)
Comparison of the Transition States for Folding of Two Ig-like Proteins from Different Superfamilies
CD Geierhaas, E Paci, M Vendruscolo, J Clarke
– Journal of Molecular Biology
(2004)
343,
1111
(doi: 10.1016/j.jmb.2004.08.100)
Prediction of the Absolute Aggregation Rates of Amyloidogenic Polypeptide Chains
KF DuBay, AP Pawar, F Chiti, J Zurdo, CM Dobson, M Vendruscolo
– J Mol Biol
(2004)
341,
1317
(doi: 10.1016/j.jmb.2004.06.043)
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
DM Korzhnev, X Salvatella, M Vendruscolo, AA Di Nardo, AR Davidson, CM Dobson, LE Kay
– Nature
(2004)
430,
586
(doi: 10.1038/nature02655)
Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin.
E Paci, J Gsponer, X Salvatella, M Vendruscolo
– J Mol Biol
(2004)
340,
555
(doi: 10.1016/j.jmb.2004.05.009)
Determination of protein structures consistent with NMR order parameters
RB Best, M Vendruscolo
– J Am Chem Soc
(2004)
126,
8090
(doi: 10.1021/ja0396955)
Reconstruction of protein structures from a vectorial representation
M Porto, U Bastolla, HE Roman, M Vendruscolo
– Physical review letters
(2004)
92,
218101
Reconstruction of protein structures from a vectorial representation.
M Porto, U Bastolla, HE Roman, M Vendruscolo
– Phys Rev Lett
(2004)
92,
218101
(doi: 10.1103/PhysRevLett.92.218101)
  • <
  • 73 of 80
  • >

Research Groups

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk

    Study at Cambridge

    About the University

    Research at Cambridge