Professor Sir Alan Fersht FRS | Page 19 | 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

Relationship of Leffler (Bronsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates (vol 101, pg 14338, 2004)

AR Fersht

– Proceedings of the National Academy of Sciences

(2004)

101,

16081

(doi: 10.1073/pnas.0407342101)

Relationship of Leffler (Bronsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates

AR Fersht

– Proc Natl Acad Sci U S A

(2004)

101,

14338

(doi: 10.1073/pnas.0406091101)

Regulation of DNA binding of p53 by its C-terminal domain.

RL Weinberg, SMV Freund, DB Veprintsev, M Bycroft, AR Fersht

– Journal of molecular biology

(2004)

342,

801

(doi: 10.1016/j.jmb.2004.07.042)

Cooperative binding of tetrameric p53 to DNA

RL Weinberg, DB Veprintsev, AR Fersht

– J Mol Biol

(2004)

341,

1145

(doi: 10.1016/j.jmb.2004.06.071)

Helix stability in barstar peptides

AS Soler-González, AR Fersht

– European journal of biochemistry

(2004)

249,

724

(doi: 10.1111/j.1432-1033.1997.t01-1-00724.x)

Carl-Ivar Branden - 1934-2004 - Obituary

SG Zhang, A Rich, JL Sussman, AR Fersht

– Nature Structural & Molecular Biology

(2004)

11,

490

(doi: 10.1038/nsmb0604-490)

Designing a metal-binding site in the scaffold of Escherichia coli KDO8PS

Z Oliynyk, L Briseño-Roa, T Janowitz, P Sondergeld, AR Fersht

– Protein Engineering, Design and Selection

(2004)

17,

383

(doi: 10.1093/protein/gzh046)

Φ-Value analysis and the nature of protein-folding transition states

AR Fersht, S Sato

– Proc Natl Acad Sci U S A

(2004)

101,

7976

(doi: 10.1073/pnas.0402684101)

Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation

P Jemth, S Gianni, R Day, B Li, CM Johnson, V Daggett, AR Fersht

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

(2004)

101,

6450

(doi: 10.1073/pnas.0401732101)

Testing protein-folding simulations by experiment: B domain of protein A.

S Sato, TL Religa, V Daggett, AR Fersht

– Proceedings of the National Academy of Sciences

(2004)

101,

6952

(doi: 10.1073/pnas.0401396101)