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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

Proton linkage of complex formation between cytochrome c and cytochrome b5: electrostatic consequences of protein-protein interactions
MR Mauk, PD Barker, AG Mauk
– Biochemistry
(2002)
30,
9873
Proton titration curve of yeast iso-1-ferricytochrome c. Electrostatic and conformational effects of point mutations.
PD Barker, MR Mauk, AG Mauk
– Biochemistry
(2002)
30,
2377
REDUCTION OF HORSE HEART FERRICYTOCHROME-C BY BOVINE LIVER FERROCYTOCHROME-B5 - EXPERIMENTAL AND THEORETICAL-ANALYSIS
LD Eltis, RG Herbert, PD Barker, AG Mauk, SH Northrup
– Biochemistry
(2002)
30,
3663
Conversion of Cytochrome b562 to c-Type Cytochromes
PD Barker, EP Nerou, SM Freund, IM Fearnley
– Biochemistry
(2002)
34,
15191
Electrochemical, kinetic, and circular dichroic consequences of mutations at position 82 of yeast iso-1-cytochrome c
SP Rafferty, LL Pearce, PD Barker, JG Guillemette, CM Kay, M Smith, AG Mauk
– Biochemistry
(2002)
29,
9365
Direct Electrochemistry of Protein-Protein Complexes Involving Cytochrome c, Cytochrome b5, and Plastocyanin
S Bagby, PD Barker, LH Guo, HA Hill
– Biochemistry
(2002)
29,
3213
pH-Linked Conformational Regulation of a Metalloprotein Oxidation-Reduction Equilibrium: Electrochemical Analysis of the Alkaline Form of Cytochrome c
PD BARKER, AG MAUK
– Journal of the American Chemical Society
(2002)
114,
3619
Effects of Charged Amino Acid Mutations on the Bimolecular Kinetics of Reduction of Yeast Iso-l-ferricytochrome c by Bovine Ferrocytochrome b5
SH Northrup, KA Thomasson, CM Miller, PD Barker, LD Eltis, JG Guillemette, SC Inglis, AG Mauk
– Biochemistry
(2002)
32,
6613
The C terminus of apocytochrome b562 undergoes fast motions and slow exchange among ordered conformations resembling the folded state
N D'Amelio, AMJJ Bonvin, M Czisch, P Barker, R Kaptein
– Biochemistry
(2002)
41,
5505
A further clue to understanding the mobility of mitochondrial yeast cytochrome c -: A 15N T1ρ investigation of the oxidized and reduced species
PD Barker, I Bertini, R Del Conte, SJ Ferguson, P Hajieva, E Tomlinson, P Turano, MS Viezzoli
– European Journal of Biochemistry
(2001)
268,
4468
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Research Group

Research Interest Groups

Telephone number

01223 763096

Email address

pdb30@cam.ac.uk