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Dr Paul Barker

Portrait of pdb30

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.

 

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

Publications

Investigating the Mechanisms of Amylolysis of Starch Granules by Solution-State NMR.
AJ Baldwin, DL Egan, FJ Warren, PD Barker, CM Dobson, PJ Butterworth, PR Ellis – Biomacromolecules (2015) 150327135128001
Theory and Practice: Bulk Synthesis of C 3 B and its H 2 - and Li-Storage Capacity
TC King, PD Matthews, H Glass, JA Cormack, JP Holgado, M Leskes, JM Griffin, OA Scherman, PD Barker, CP Grey, SE Dutton, RM Lambert, G Tustin, A Alavi, DS Wright – Angew Chem Int Ed Engl (2015) n/a
Selective Lability of Ruthenium(II) Arene Amino Acid Complexes.
TG Scrase, MJ O'Neill, AJ Peel, PW Senior, PD Matthews, H Shi, SR Boss, PD Barker – Inorg Chem (2015) 54, 3118
Folates are potential ligands for ruthenium compounds in vivo.
TG Scrase, SM Page, PD Barker, SR Boss – Dalton transactions (Cambridge, England : 2003) (2014) 43, 8158
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
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
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
Continued surprises in the cytochrome c biogenesis story
EB Sawyer, PD Barker – Protein & Cell (2012) 3, 405
Structural basis for efficient chromophore communication and energy transfer in a constructed didomain protein scaffold
JA Arpino, H Czapinska, A Piasecka, WR Edwards, P Barker, MJ Gajda, M Bochtler, DD Jones – Journal of the American Chemical Society (2012) 134, 13632
Metastability of native proteins and the phenomenon of amyloid formation.
AJ Baldwin, TP 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
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Research Group

Research Interest Groups

Telephone number

01223 763096

Email address

pdb30@cam.ac.uk