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Yusuf Hamied Department of Chemistry

 

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

Pathway and stability of protein folding.
AR Fersht, M Bycroft, A Horovitz, JT Kellis, A Matouschek, L Serrano
– Philosophical Transactions of the Royal Society B Biological Sciences
(1997)
332,
171
Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution
AR Fersht
– Philosophical Transactions of the Royal Society B Biological Sciences
(1997)
348,
11
Catalysis, binding and enzyme-substrate complementarity.
AR Fersht
– Proceedings of the Royal Society of London. Series B. Biological Sciences
(1997)
187,
397
Structure and activity of the tyrosy1-tRNA synthetase: the hydrogen bond in catalysis and specificity
AR FERSHT, RJ LEATHERBARROW, TNC WELLS
– Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences
(1997)
317,
305
INTRODUCTORY-REMARKS TO THE 3RD SESSION
AR FERSHT
– Philosophical Transactions of the Royal Society of London B Biological Sciences
(1997)
293,
119
Preface
CM DOBSON, AR FERSHT
– Philosophical Transactions of the Royal Society B Biological Sciences
(1997)
348,
3
Enzymic editing mechanisms and the genetic code.
AR Fersht
– Proceedings of the Royal Society of London. Series B, Biological sciences
(1997)
212,
351
Strain in the folding nucleus of chymotrypsin inhibitor 2
AG Ladurner, LS Itzhaki, AR Fersht
– Structure
(1997)
2,
363
Hydrogen exchange at equilibrium: A short cut for analysing pathways?
J Clarke, LS Itzhaki, AR Fersht
– Trends Biochem Sci
(1997)
22,
284
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
R Zahn, AM Buckle, S Perrett, CM Johnson, FJ Corrales, R Golbik, AR Fersht
– Proc Natl Acad Sci U S A
(1996)
93,
15024
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