Award details

Establishment of a core facility for circular dichroism spectroscopy

Reference	REI18433
Principal Investigator / Supervisor	Professor Daniel Aeschlimann
Co-Investigators / Co-Supervisors	Dr Konrad Beck, Professor Ruth Duncan, Professor Michael Ehrmann, Professor Bryan Morgan
Institution	Cardiff University
Department	Division of Clinical Laboratory Science
Funding type	Research
Value (£)	51,780
Status	Completed
Type	Research Grant
Start date	01/04/2003
End date	31/03/2004
Duration	12 months

Abstract

The establishment of a core facility for circular dichroism (CD) spectroscopy would facilitate and enhance the research programs of a number of BBSRC supported researchers within the Cardiff Bioscience community. The instrument will complement a number of existing technologies relevant to proteomics including MALDI-TOF, surface plasmon resonance spectroscopy, atomic force microscopy, and molecular force probe, and is expected to form the protein arm of the recently established Central Biotechnology Services at UWCM. Because of the nature of a multi-user facility the projects in this application are thematically diverse and are concerned with proteins regulating extracellular matrix assembly and cell-matrix interactions, proteins of the complement system, mediators of the folding process during protein biosynthesis as well as protein-polymer conjugates in drug delivery. Some of our research projects are biophysically orientated, while others with a molecular biology or molecular medicine focus have increasingly the need to complement functional studies with structural characterisations at different levels. Identifying structural changes in proteins due to posttranslational modifications or modifications introduced by chemical and genetic engineering are of critical importance for data interpretation. Thermal de- and renaturation experiments provide an insight into the folding and stability of proteins under various conditions, and for finding of appropriate conditions for the refolding of proteins which can only be isolated under denaturing conditions. CD spectroscopy is unique in that it provides a relatively simple and cost effective means to directly monitor structural changes in proteins where only a limited amount of material is available. Easy access to this technology will have a significant impact on our current and future research projects.

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 2002 (REI) [2002]
Funding Scheme	X – not Funded via a specific Funding Scheme

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