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Yusuf Hamied Department of Chemistry

 

University Associate Professor

Research in my group can be divided into two areas, although these share a common theme of engineering metal protein interactions in novel ways.

One goal is to engineer novel proteins and polypeptide based assemblies that can be used in molecular electronic devices and nanotechnology in general. This involves understanding, at a fundamental level, how metal cofactors, particularly heme, is delivered to proteins in vivo and, in the case of c-type cytochromes, how heme is covalently attached to protein. It also involves understanding how functional protein units can be assembled into larger nanoscale assemblies that gain function through the proximity of the constituent monomers.

The other goal is to explore the interaction of 4d and 5d transition metals with proteins, particularly as a possible route to finding novel medicinal compounds. Specifically, Ruthenium organometallic complexes have shown some potential as anti cancer compounds, but little is understood about how the chemistry of Ruthenium interacts with biomolecules.

Research Interests

  • Self Assembly of Proteins into functional materials
  • Heme protein assembly and heme chaperones
  • Electrochemistry of Proteins
  • Heavy metal complexes and ther interaction with Proteins

Watch Dr Barker discuss his research

Publications

Cytochrome Display on Amyloid Fibrils
AJ Baldwin, R Bader, J Christodoulou, CE MacPhee, CM Dobson, PD Barker
– Journal of the American Chemical Society
(2006)
128,
2162
Controlling Self‐Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme
DD Jones, PD Barker
– Angewandte Chemie International Edition
(2005)
44,
6337
Why isn't 'standard' heme good enough for c-type and d1-type cytochromes?
JWA Allen, PD Barker, O Daltrop, JM Stevens, EJ Tomlinson, N Sinha, Y Sambongi, SJ Ferguson
– Dalton Transactions
(2005)
3410
Electron transfer reactions of metalloproteins at peptide-modified gold electrodes.
PD Barker, K Di Gleria, HA Hill, VJ Lowe
– The FEBS Journal
(2005)
190,
171
Organisation of recombinant lipid-tagged cytochrome on surface
P Kreutzmann, M Manzanera, J Norris, R Michael, M Moreau, WTS Huck, PD Barker
– BIOPHYSICAL JOURNAL
(2005)
88,
394A
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
P Garcia, M Bruix, M Rico, S Ciofi-Baffoni, L Banci, MC Ramachandra Shastry, H Roder, T de Lumley Woodyear, CM Johnson, AR Fersht, PD Barker
– J Mol Biol
(2004)
346,
331
Design and characterisation of an artificial DNA-binding cytochrome
DD Jones, PD Barker
– Chembiochem
(2004)
5,
964
A Cytochrome b562 Variant with a c-Type Cytochrome CXXCH: Heme-binding Motif as a Probe of the Escherichia coli Cytochrome c Maturation System
JWA Allen, PD Barker, SJ Ferguson
– J Biol Chem
(2003)
278,
52075
Designing redox metalloproteins from bottom-up and top-down perspectives.
PD Barker
– Curr Opin Struct Biol
(2003)
13,
490
Solution structure and characterization of the heme chaperone CcmE
F Arnesano, L Banci, PD Barker, I Bertini, A Rosato, XC Su, MS Viezzoli
– Biochemistry
(2002)
41,
13587
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Research Group

Research Interest Groups

Telephone number

01223 763096

Email address

pdb30@cam.ac.uk