skip to content

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

Hot-spot mutants of p53 core domain evince characteristic local structural changes.
KB Wong, BS DeDecker, SM Freund, MR Proctor, M Bycroft, AR Fersht
– Proc Natl Acad Sci U S A
(1999)
96,
8438
Equilibrium folding properties of the yeast prion protein determinant Ure211Edited by J. Karn
S Perrett, SJ Freeman, PJ Butler, AR Fersht
– Journal of Molecular Biology
(1999)
290,
331
The Solution Structure of Oxidized Escherichia coli Cytochrome b562,
F Arnesano, L Banci, I Bertini, J Faraone-Mennella, A Rosato, PD Barker, AR Fersht
– Biochemistry
(1999)
38,
8657
Minimal and optimal mechanisms for GroE-mediated protein folding (vol 95, pg 15275, 1998)
AP Ben-Zvi, J Chatellier, AR Fersht, P Goloubinoff
– PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(1999)
96,
5890
Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization
MG Mateu, AR Fersht
– Proc Natl Acad Sci U S A
(1999)
96,
3595
Acquisition of native-like interactions in C-terminal fragments of barnase.
JL Neira, AR Fersht
– J Mol Biol
(1999)
287,
421
Structural response to mutation at a protein-protein interface11Edited by R. Huber
CK Vaughan, AM Buckle, AR Fersht
– Journal of molecular biology
(1999)
286,
1487
An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase
DD Axe, NW Foster, AR Fersht
– Journal of Molecular Biology
(1999)
286,
1471
Oxidative refolding chromatography: folding of the scorpion toxin Cn5.
MM Altamirano, C García, LD Possani, AR Fersht
– Nature biotechnology
(1999)
17,
187
(doi: 10.1038/6192)
Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53
MG Mateu, MM Sánchez Del Pino, AR Fersht
– Nat Struct Biol
(1999)
6,
191
(doi: 10.1038/5880)
  • <
  • 41 of 66
  • >