Professor Sir Alan Fersht FRS | Page 18 | Yusuf Hamied Department of Chemistry

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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

Modulation of binding of DNA to the C-terminal domain of p53 by acetylation.

A Friedler, DB Veprintsev, SMV Freund, KI von Glos, AR Fersht

– Structure (London, England : 1993)

(2005)

13,

629

(doi: 10.1016/j.str.2005.01.020)

Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor

MR Fernandez-Fernandez, DB Veprintsev, AR Fersht

– Proc Natl Acad Sci U S A

(2005)

102,

4735

(doi: 10.1073/pnas.0501459102)

Insertion in barnase of a loop sequence from ribonuclease T1. Investigating sequence and structure alignments by protein engineering.

S Vuilleumier, AR Fersht

– The FEBS Journal

(2005)

221,

1003

(doi: 10.1111/j.1432-1033.1994.tb18817.x)

Structures of p53 Cancer Mutants and Mechanism of Rescue by Second-site Suppressor Mutations*

AC Joerger, HC Ang, DB Veprintsev, CM Blair, AR Fersht

– The Journal of biological chemistry

(2005)

280,

16030

(doi: 10.1074/jbc.M500179200)

Binding of Natively Unfolded HIF-1α ODD Domain to p53

N Sánchez-Puig, DB Veprintsev, AR Fersht

– Molecular Cell

(2005)

17,

11

(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)

33,

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

– Journal of molecular biology

(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)

Phi value versus psi analysis.

AR Fersht

– Proc Natl Acad Sci U S A

(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)