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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

Tuning heavy metal compounds for anti-tumor activity: is diversity the key to ruthenium's success?
SM Page, SR Boss, PD Barker
– Future Medicinal Chemistry
(2009)
1,
541
Interfacial redox processes of cytochrome b(562)
P Zuo, T Albrecht, PD Barker, DH Murgida, P Hildebrandt
– Physical Chemistry Chemical Physics
(2009)
11,
7430
Variant c-type cytochromes as probes of the substrate specificity of the E. coli cytochrome c maturation (Ccm) apparatus
JWA Allen, EB Sawyer, ML Ginger, PD Barker, SJ Ferguson
– Biochemical Journal
(2009)
419,
177
Measurement of Amyloid Fibril Length Distributions by Inclusion of Rotational Motion in Solution NMR Diffusion Measurements
AJ Baldwin, SJ Anthony‐Cahill, TPJ Knowles, G Lippens, J Christodoulou, PD Barker, CM Dobson
– Angewandte Chemie
(2008)
120,
3433
Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements.
AJ Baldwin, SJ Anthony-Cahill, TPJ Knowles, G Lippens, J Christodoulou, PD Barker, CM Dobson
– Angewandte Chemie International Edition
(2008)
47,
3385
Contribution of rotational diffusion to pulsed field gradient diffusion measurements.
AJ Baldwin, J Christodoulou, PD Barker, CM Dobson, G Lippens
– Journal of Chemical Physics
(2007)
127,
114505
An induced-fit conformational change underlies the binding mechanism of the heme-transport Proteobacteria-protein HemS
M Paoli, S Schneider, K Sharp, P Barker
– FASEB JOURNAL
(2007)
21,
A242
An induced fit conformational change underlies the binding mechanism of the heme transport proteobacteria-protein HemS.
S Schneider, KH Sharp, PD Barker, M Paoli
– J Biol Chem
(2006)
281,
32606
Crystal structure of the bacterial protein HemS in complex with haem
S Schneider, P Barker, K Sharp, M Paoli
– Acta Crystallographica Section A: Foundations and advances
(2006)
62,
S179
Macroscopic 2D Networks Self-Assembled from Nanometer-Sized Protein/DNA Complexes
M Manzanera, DJ Frankel, H Li, D Zhou, A Bruckbauer, P Kreutzmann, JM Blackburn, C Abell, T Rayment, D Klenerman, PD Barker
– Nano Lett
(2006)
6,
365
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Research Group

Research Interest Groups

Telephone number

01223 763096

Email address

pdb30@cam.ac.uk