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

Crystallographic analysis of Phe-->Leu substitution in the hydrophobic core of barnase.

YW Chen, AR Fersht, K Henrick

Acta Crystallographica Section D, Structural Biology

(1995)

220

(doi: 10.1107/s0907444994008851)

Characterizing transition states in protein folding: an essential step in the puzzle

AR Fersht

Current opinion in structural biology

(1995)

(doi: 10.1016/0959-440x(95)80012-p)

ASSOCIATION OF PROTEIN-FRAGMENTS THROUGH A 2ND-ORDER FOLDING REACTION - STRUCTURE OF THE ISOLATED FRAGMENTS AND EARLY EVENTS OF PROTEIN-FOLDING

GD GAV, J RUIZSANZ, B DAVIS, AR FERSHT

PROTEIN ENGINEERING

(1995)

THE STRUCTURE OF THE TRANSITION-STATE FOR THE ASSOCIATION OF 2 FRAGMENTS OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 TO GENERATE NATIVE-LIKE PROTEIN - IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING

G de Prat Gay, J Ruiz-Sanz, B Davis, AR Fersht

Proceedings of the National Academy of Sciences

(1994)

10943

(doi: 10.1073/pnas.91.23.10943)

Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.

DE Otzen, LS Itzhaki, NF elMasry, SE Jackson, AR Fersht

Proc Natl Acad Sci U S A

(1994)

10422

(doi: 10.1073/pnas.91.22.10422)

Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.

AR Fersht, LS Itzhaki, NF elMasry, JM Matthews, DE Otzen

Proceedings of the National Academy of Sciences

(1994)

10426

(doi: 10.1073/pnas.91.22.10426)

STABILITY AND FUNCTION - 2 CONSTRAINTS IN THE EVOLUTION OF BARSTAR AND OTHER PROTEINS