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 tranistion 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.
Local Frustration Determines Molecular and Macroscopic Helix Structures
CJ Forman, SN Fejer, D Chakrabarti, PD Barker, DJ Wales - J Phys Chem B (
2013)
117, 7918
(DOI:
10.1021/jp4040503)
Probing the location of displayed cytochrome b562 on amyloid by scanning tunnelling microscopy
CJ Forman, N Wang, ZY Yang, CG Mowat, S Jarvis, C Durkan, PD Barker - Nanotechnology (
2013)
24, 175102
(DOI:
10.1088/0957-4484/24/17/175102)
Structural basis for efficient chromophore communication and energy transfer in a constructed didomain protein scaffold
JAJ Arpino, H Czapinska, A Piasecka, WR Edwards, P Barker, MJ Gajda, M Bochtler, DD Jones - Journal of the American Chemical Society (
2012)
134, 13632
(DOI:
10.1021/ja301987h)
Continued surprises in the cytochrome c biogenesis story
EB Sawyer, PD Barker - Protein & Cell (
2012)
3, 405
(DOI:
10.1007/s13238-012-2912-x)
The morphology of decorated amyloid fibers is controlled by the conformation and position of the displayed protein
CJ Forman, AA Nickson, SJ Anthony-Cahill, AJ Baldwin, G Kaggwa, U Feber, K Sheikh, SP Jarvis, PD Barker - ACS Nano (
2012)
6, 1332
(DOI:
10.1021/nn204140a)
Metastability of native proteins and the phenomenon of amyloid formation.
AJ Baldwin, TPJ Knowles, GG Tartaglia, AW Fitzpatrick, GL Devlin, SL Shammas, CA Waudby, MF Mossuto, S Meehan, SL Gras, J Christodoulou, SJ Anthony-Cahill, PD Barker, M Vendruscolo, CM Dobson - Journal of the American Chemical Society (
2011)
133, 14160
(DOI:
10.1021/ja2017703)
Metal and redox selectivity of protoporphyrin binding to the heme chaperone CcmE.
EM Harvat, O Daltrop, F Sobott, M Moreau, PD Barker, JM Stevens, SJ Ferguson - Metallomics (
2011)
3, 363
(DOI:
10.1039/c0mt00085j)
Aberrant attachment of heme to cytochrome by the Ccm system results in a cysteine persulfide linkage.
EB Sawyer, E Stephens, SJ Ferguson, JWA Allen, PD Barker - Journal of the American Chemical Society (
2010)
132, 4974
(DOI:
10.1021/ja908241v)
Interfacial redox processes of cytochrome b562.
P Zuo, T Albrecht, PD Barker, DH Murgida, P Hildebrandt - Physical Chemistry Chemical Physics (
2009)
11, 7430
(DOI:
10.1039/b904926f)
Tuning heavy metal compounds for anti-tumor activity: is diversity the key to ruthenium's success?
SM Page, SR Boss, PD Barker - Future Med Chem (
2009)
1, 541
(DOI:
10.4155/FMC.09.25)
