Award details

Linear dichroism for realtime small volume analysis of biomacromolecule structure and ligand binding

Reference	REI20503
Principal Investigator / Supervisor	Professor Alison Rodger
Co-Investigators / Co-Supervisors	Professor Timothy Bugg, Professor Timothy Dafforn, Dr David Halsall, Professor Michael Hannon, Professor Colin Robinson, Professor Dek Woolfson
Institution	University of Warwick
Department	Chemistry
Funding type	Research
Value (£)	66,700
Status	Completed
Type	Research Grant
Start date	24/11/2003
End date	23/11/2004
Duration	12 months

Abstract

The aim of this proposal is to set up a unique spectroscopic facility at the the University of Warwick that will provide new insights into the structure of a wide range of biomacromolecules. This facility will be based on linear dichroism (LD) and will exploit recent advances made at Warwick in the design of a novel sample cell based on a couette geometry that substantially reduces the volume of sample needed for assay and also enables temperature control. There exists now the potential for a range of new applications for LD to provide new insights and understanding hitherto inaccessible by other techniques. LD is the ideal technique for determining the orientations of biomolecular systems that can be oriented by shear forces. Examples of such applications include membrane proteins in liposomes, fibrous proteins, polymerising proteins and nucleic acids, all with or without bound ligand. The PI and the Co-Applicants will then collaborate, in a series of sub-projects to apply the instrument to a specific system. Funding for these sub-projects, which will be co-ordinated by the Co-Applicants aleady exists from other sources. The sub-projects include: 1. DNA binding and DNA intramolecular coiling by metallo-helicates, where one of the goals is sequence specific DNA structure control by designer molecules. 2. Membrane protein insertion and translocation, for which LD provides a fast indication of protein orientation in model membrame systems. 3. Designed peptide fibres, where the new applications in the area of nanobiotechnology will be facilitated by the structural characterisation provided by LD for the fibres. 4. Structure and kinetics of formation of naturally occurring fibres for which the advances in LD are proving to be ideal for helping identify the orientations of monomer units in the fibres and ligands bound to fibres, as well as for following the kinetics of fibre formation and depolymerisation. 5. LD as a probe for real time polymerase chain reaction detection, with the particular aim of high-throughput clinical analysis. 6. Molecular mechanism of the bacteriolytic E protein from bacteriophage 174, where the principal applicants recent work on determining orientation of proteins on and in liposomes will be applied to probe the structure of protein-protein and protein-ligand complexes. Although not intended as the main use, the new instrument will also facilitate small volume capillary circular dichroism (CD) measurements recently initiated at Warwick.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	Research Equipment Initiative 2003 (RE2) [2003]
Funding Scheme	X – not Funded via a specific Funding Scheme

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