Professor Sir Alan Fersht FRS | Page 20 | 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

The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid

T Batuwangala, D Shepherd, SD Gadola, KJC Gibson, NR Zaccai, AR Fersht, GS Besra, V Cerundolo, EY Jones

– J Immunol

(2004)

172,

2382

(doi: 10.4049/jimmunol.172.4.2382)

Binding of p53-derived Ligands to MDM2 Induces a Variety of Long Range Conformational Changes

O Schon, A Friedler, S Freund, AR Fersht

– J Mol Biol

(2004)

336,

197

(doi: 10.1016/j.jmb.2003.11.051)

Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: Implications for "Mutant conformation"

A Friedler, BS DeDecker, SMV Freund, C Blair, S Rüdiger, AR Fersht

– J Mol Biol

(2004)

336,

187

(doi: 10.1016/j.jmb.2003.12.005)

Analysis of Enzyme Structure and Activity by Protein Engineering

AR FERSHT, JP SHI, AJ WILKINSON, DM BLOW, P CARTER, MMY WAYE, GP WINTER

– Angewandte Chemie International Edition

(2003)

23,

467

(doi: 10.1002/anie.198404673)

Structural insights in the folding of small single-domain proteins.

S Gianni, U Mayor, AR Fersht

– Ital J Biochem

(2003)

52,

154

(link to publication)

The Denatured State of Engrailed Homeodomain under Denaturing and Native Conditions

U Mayor, JG Grossmann, NW Foster, SMV Freund, AR Fersht

– Journal of molecular biology

(2003)

333,

977

(doi: 10.1016/j.jmb.2003.08.062)

Unifying features in protein-folding mechanisms

S Gianni, NR Guydosh, F Khan, TD Caldas, U Mayor, GWN White, ML DeMarco, V Daggett, AR Fersht

– Proceedings of the National Academy of Sciences

(2003)

100,

13286

(doi: 10.1073/pnas.1835776100)

Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide

N Issaeva, A Friedler, P Bozko, KG Wiman, AR Fersht, G Selivanova

– Proceedings of the National Academy of Sciences of the United States of America

(2003)

100,

13303

(doi: 10.1073/pnas.1835733100)

The kinetic pathway of folding of barnase.

F Khan, JI Chuang, S Gianni, AR Fersht

– J Mol Biol

(2003)

333,

169

(doi: 10.1016/j.jmb.2003.08.024)

Crystal structure of a superstable mutant of human p53 core domain - Insights into the mechanism of rescuing oncogenic mutations

AC Joerger, MD Allen, AR Fersht

– J Biol Chem

(2003)

279,

1291

(doi: 10.1074/jbc.m309732200)