Professor Sir Alan Fersht FRS

Our major research programme concerns the folding, stability and activity of proteins. We apply a broad multi-disciplinary approach that combines methods and ideas of molecular biology and physical-organic chemistry. We use techniques including protein engineering, DNA cloning, sequencing and mutagenesis, cell culture, gene and peptide synthesis, spectroscopy, rapid reaction techniques, multi-dimensional NMR (we have a 500, 600, 700 and an 800 MHz spectrometers) and x-ray protein crystallography.

Current major projects include: protein folding, misfolding and disease; drug discovery; and structure-activity relationships of proteins involved in cancer and disease.

Although now emeritus, I am still fully active in research with long term funding, including an MRC Programme Grant.

Publications

Binding of natively unfolded HIF-1 alpha ODD domain to p53

N Sánchez-Puig, DB Veprintsev, AR Fersht

Molecular cell

(2005)

(doi: 10.1016/j.molcel.2004.11.019)

PFD: a database for the investigation of protein folding kinetics and stability

KF Fulton, GL Devlin, RA Jodun, L Silvestri, SP Bottomley, AR Fersht, AM Buckle

Nucleic Acids Res

(2005)

d279

(doi: 10.1093/nar/gki016)

Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562

P Garcia, M Bruix, M Rico, S Ciofi-Baffoni, L Banci, MC Ramachandra Shastry, H Roder, T de Lumley Woodyear, CM Johnson, AR Fersht, PD Barker

J Mol Biol

(2004)

346

331

(doi: 10.1016/j.jmb.2004.11.044)

Binding of Rad51 and other peptide sequences to a promiscuous, highly electrostatic binding site in p53

A Friedler, DB Veprintsev, T Rutherford, KI von Glos, AR Fersht

J Biol Chem

(2004)

280

8051

(doi: 10.1074/jbc.m411176200)

Φ value versus ψ analysis

AR Fersht

Proceedings of the National Academy of Sciences

(2004)

101

17327

(doi: 10.1073/pnas.0407863101)

One-state downhill versus conventional protein folding

N Ferguson, PJ Schartau, TD Sharpe, S Sato, AR Fersht

Journal of molecular biology

(2004)

344

295

(doi: 10.1016/j.jmb.2004.09.069)

Relationship of Leffler (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates (vol 101, pg 14338, 2004)

AR Fersht

Proceedings of the National Academy of Sciences

(2004)

101

16081

(doi: 10.1073/pnas.0407342101)

Relationship of Leffler (Brønsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates

AR Fersht

Proceedings of the National Academy of Sciences

(2004)

101

14338