skip to content
Home

Yusuf Hamied Department of Chemistry

 

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

Characterizing transition states in protein folding: an essential step in the puzzle.
AR Fersht
– Current Opinion in Structural Biology
(1995)
5,
79
(doi: 10.1016/0959-440x(95)80012-p)
Folding & Design: introduction to a new journal
AR Fersht, FE Cohen
– Structure
(1995)
1,
i
(doi: 10.1016/s1359-0278(96)00001-6)
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)
8,
19
(link to publication)
The structure of the transition state for the association of two 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 of the United States of America
(1994)
91,
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
– Proceedings of the National Academy of Sciences of the United States of America
(1994)
91,
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
– Proc Natl Acad Sci U S A
(1994)
91,
10426
(doi: 10.1073/pnas.91.22.10426)
STABILITY AND FUNCTION - 2 CONSTRAINTS IN THE EVOLUTION OF BARSTAR AND OTHER PROTEINS
G Schreiber, AM Buckle, AR Fersht
– Structure (London, England : 1993)
(1994)
2,
945
(doi: 10.1016/s0969-2126(94)00096-4)
TOWARD SOLVING THE FOLDING PATHWAY OF BARNASE - THE COMPLETE BACKBONE C-13, N-15, AND H-1-NMR ASSIGNMENTS OF ITS PH-DENATURED STATE
VL Arcus, S Vuilleumier, SM Freund, M Bycroft, AR Fersht
– Proc Natl Acad Sci U S A
(1994)
91,
9412
(doi: 10.1073/pnas.91.20.9412)
Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
A Matouschek, JM Matthews, CM Johnson, AR Fersht
– Protein Engineering Design and Selection
(1994)
7,
1089
(doi: 10.1093/protein/7.9.1089)
Mutational analysis of the N-capping box of the alpha-helix of chymotrypsin inhibitor 2.
NF elMasry, AR Fersht
– Protein Engineering Design and Selection
(1994)
7,
777
(doi: 10.1093/protein/7.6.777)
  • <
  • 52 of 66
  • >

    Study at Cambridge

    About the University

    Research at Cambridge