Professor Sir Alan Fersht FRS | Page 15 | 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

Structure-function-rescue: the diverse nature of common p53 cancer mutants

AC Joerger, AR Fersht

– Oncogene

(2007)

26,

2226

(doi: 10.1038/sj.onc.1210291)

Conformational entropy of alanine versus glycine in protein denatured states

KA Scott, DOV Alonso, S Sato, AR Fersht, V Daggett

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

(2007)

104,

2661

(doi: 10.1073/pnas.0611182104)

Structural biology: analysis of 'downhill' protein folding.

N Ferguson, TD Sharpe, CM Johnson, PJ Schartau, AR Fersht

– Nature

(2007)

445,

e14

(doi: 10.1038/nature05643)

Folding and binding: implementing the game plan - Editorial overview

AR Fersht, V Daggett

– Current Opinion in Structural Biology

(2007)

17,

1

(doi: 10.1016/j.sbi.2007.01.011)

Distinguishing between cooperative and unimodal downhill protein folding

F Huang, S Sato, TD Sharpe, L Ying, AR Fersht

– Proceedings of the National Academy of Sciences

(2007)

104,

123

(doi: 10.1073/pnas.0609717104)

Structural Biology of the Tumor Suppressor p53 and Cancer‐Associated Mutants

AC Joerger, AR Fersht

– Advances in cancer research

(2007)

97,

1

(doi: 10.1016/s0065-230x(06)97001-8)

General structural motifs of amyloid protofilaments (vol 103, pg 16248, 2006)

N Ferguson, J Becker, H Tidow, S Tremmel, TD Sharpe, G Krause, J Flinders, M Petrovich, J Berriman, H Oschkinat, AR Fersht

– P NATL ACAD SCI USA

(2006)

103,

18875

(link to publication)

Pro-sequence-assisted protein folding.

J Eder, AR Fersht

– Molecular microbiology

(2006)

16,

609

(doi: 10.1111/j.1365-2958.1995.tb02423.x)

General structural motifs of amyloid protofilaments

N Ferguson, J Becker, H Tidow, S Tremmel, TD Sharpe, G Krause, J Flinders, M Petrovich, J Berriman, H Oschkinat, AR Fersht

– Proceedings of the National Academy of Sciences

(2006)

103,

16248

(doi: 10.1073/pnas.0607815103)

Structural basis for understanding oncogenic p53 mutations and designing rescue drugs

AC Joerger, HC Ang, AR Fersht

– Proc Natl Acad Sci U S A

(2006)

103,

15056

(doi: 10.1073/pnas.0607286103)