Professor Sir Alan Fersht FRS | Page 12 | Yusuf Hamied Department of Chemistry

skip to content

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

Interfaces: two worlds unite.

J-M Lehn, AR Fersht

– Chembiochem : a European journal of chemical biology

(2008)

10,

4

(doi: 10.1002/cbic.200800740)

Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p53

TS Wong, S Rajagopalan, FM Townsley, SM Freund, M Petrovich, D Loakes, AR Fersht

– Nucleic Acids Research

(2008)

37,

568

(doi: 10.1093/nar/gkn974)

Structure of Human MDM4 N-Terminal Domain Bound to a Single-Domain Antibody

GW Yu, M Vaysburd, MD Allen, G Settanni, AR Fersht

– Journal of molecular biology

(2008)

385,

1578

(doi: 10.1016/j.jmb.2008.11.043)

Structural biology of the tumor suppressor p53.

AC Joerger, AR Fersht

– Annual Review of Biochemistry

(2008)

77,

557

(doi: 10.1146/annurev.biochem.77.060806.091238)

14-3-3 activation of DNA binding of p53 by enhancing its association into tetramers

S Rajagopalan, AM Jaulent, M Wells, DB Veprintsev, AR Fersht

– Nucleic Acids Res

(2008)

36,

5983

(doi: 10.1093/nar/gkn598)

PHYS 27-Experimental resolution of the early events in the folding of B domain of Protein A

DM Vu, SH Brewer, S Sato, AR Fersht, RB Dyer

– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY

(2008)

236,

(link to publication)

Members of the S100 family bind p53 in two distinct ways.

MR Fernandez-Fernandez, TJ Rutherford, AR Fersht

– Protein Sci

(2008)

17,

1663

(doi: 10.1110/ps.035527.108)

A Sequential Assignment Procedure for Proteins that have Intermediate Line Widths in MAS NMR Spectra: Amyloid Fibrils of Human CA150.WW2

J Becker, N Ferguson, J Flinders, B-J van Rossum, AR Fersht, H Oschkinat

– Chembiochem

(2008)

9,

1946

(doi: 10.1002/cbic.200700706)

Targeted rescue of a destabilized mutant of p53 by an in silico screened drug

FM Boeckler, AC Joerger, G Jaggi, TJ Rutherford, DB Veprintsev, AR Fersht

– Proceedings of the National Academy of Sciences

(2008)

105,

10360

(doi: 10.1073/pnas.0805326105)

The novel p53 isoform “delta p53” is a misfolded protein and does not bind the p21 promoter site

MM García-Alai, H Tidow, E Natan, FM Townsley, DB Veprintsev, AR Fersht

– Protein Sci

(2008)

17,

1671

(doi: 10.1110/ps.036996.108)