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

Combining Simulation and Experiment to Map Protein Folding

AL Jonsson, AR Fersht, V Daggett

COMPREHENSIVE BIOPHYSICS, VOL 3: THE FOLDING OF PROTEINS AND NUCLEIC ACIDS

(2012)

(doi: 10.1016/b978-0-12-374920-8.00301-5)

Evaluating Drosophila p53 as a Model System for Studying Cancer Mutations

G Herzog, AC Joerger, MD Shmueli, AR Fersht, E Gazit, D Segal

The Journal of biological chemistry

(2012)

287

44330

(doi: 10.1074/jbc.M112.417980)

Chemical physics of protein folding

PG Wolynes, WA Eaton, AR Fersht

Proceedings of the National Academy of Sciences

(2012)

109

17770

(doi: 10.1073/pnas.1215733109)

Stability of p53 Homologs

T Brandt, JL Kaar, AR Fersht, DB Veprintsev

PLoS ONE

(2012)

e47889

(doi: 10.1371/journal.pone.0047889)

Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2

SM Vogel, MR Bauer, AC Joerger, R Wilcken, T Brandt, DB Veprintsev, TJ Rutherford, AR Fersht, FM Boeckler

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

(2012)

109

16906

(doi: 10.1073/pnas.1215060109)

Sequence-dependent sliding kinetics of p53

JS Leith, A Tafvizi, F Huang, WE Uspal, PS Doyle, AR Fersht, LA Mirny, AM van Oijen

Proc Natl Acad Sci U S A

(2012)

109

16552

(doi: 10.1073/pnas.1120452109)

Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy.

M Bista, SM Freund, AR Fersht

Proceedings of the National Academy of Sciences

(2012)

109

15752

(doi: 10.1073/pnas.1214176109)

In support of the BMRB.

JL Markley, H Akutsu, T Asakura, M Baldus, R Boelens, A Bonvin, R Kaptein, A Bax, I Bezsonova, MR Gryk, JC Hoch, DM Korzhnev, MW Maciejewski, D Case, WJ Chazin, TA Cross, S Dames, H Kessler, O Lange, T Madl, B Reif, M Sattler, D Eliezer, A Fersht, J Forman-Kay, LE Kay, J Fraser, J Gross, T Kortemme, A Sali, T Fujiwara, K Gardner, X Luo, J Rizo-Rey, M Rosen, RR Gil, C Ho, G Rule, AM Gronenborn, R Ishima, J Klein-Seetharaman, P Tang, P van der Wel, Y Xu, S Grzesiek, S Hiller, J Seelig, ED Laue, H Mott, D Nietlispach, I Barsukov, L-Y Lian, D Middleton, T Blumenschein, G Moore, I Campbell, J Schnell, IJ Vakonakis, A Watts, MR Conte, J Mason, M Pfuhl, MR Sanderson, J Craven, M Williamson, C Dominguez, G Roberts, U Günther, M Overduin, J Werner, P Williamson, C Blindauer, M Crump, P Driscoll, T Frenkiel, A Golovanov, S Matthews, J Parkinson, D Uhrin, M Williams, D Neuhaus, H Oschkinat, A Ramos, DE Shaw, C Steinbeck, M Vendruscolo, GW Vuister, KJ Walters, H Weinstein, K Wüthrich, S Yokoyama

Nature Structural Molecular Biology

(2012)

854

(doi: 10.1038/nsmb.2371)

First-order rate-determining aggregation mechanism of p53 and its implications

G Wang, AR Fersht

Proceedings of the National Academy of Sciences

(2012)

109

13590

(doi: 10.1073/pnas.1211557109)

Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition.

R Wilcken, G Wang, FM Boeckler, AR Fersht

Proceedings of the National Academy of Sciences

(2012)

109

13584

(doi: 10.1073/pnas.1211550109)

Professor Sir Alan Fersht FRS

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