Details of Grant 

EPSRC Reference:	GR/R76226/01
Title:	Structure and Energetics of Peptides and Small Proteins
Principal Investigator:	Barran, Professor PE
Other Investigators:
Researcher Co-Investigators:
Project Partners:
Department:	Sch of Chemistry
Organisation:	University of Edinburgh
Scheme:	Advanced Fellowship (Pre-FEC)
Starts:	01 March 2003	Ends:	31 July 2008	Value (£):	210,003
EPSRC Research Topic Classifications:	Biological & Medicinal Chem. Chemical Structure Gas & Solution Phase Reactions
EPSRC Industrial Sector Classifications:	Pharmaceuticals and Biotechnology
Related Grants:
Panel History:	Panel Date Panel Name Outcome 23 Nov 2001 Chemistry AF & SF Sifting Panel Deferred 18 Jan 2002 Chemistry AF Interviews 2002 Deferred
Summary on Grant Application Form
This research proposal seeks to develop an ion-trap, ion mobility, quadrupole mass spectrometer, with which to study the structure, and energetics of peptides and small proteins as ions in the gas phase. Experimental work will concentrate on the influence of metal binding on protein structure and will initially examine the 'calcium triggers' Calmodulin and Calbindin, which undergo specific and well characterised physical changes on metal binding. Subsequent conformational changes occur on binding to a target receptor, (once the metal is bound) and these effects too will be investigated. The effect on tertiary structure of other metal ions binding to the calcium sites will also be investigated. By synthesising peptides that correspond to the sequence forming a metal binding site, the non-covalent interactions responsible for metal binding can be studied in more detail. Careful choice of simple ligands to mimic the binding at the metal site will provide insight into preferred co-ordination and the bonding involved. Experimental work will be supported with molecular mechanics calculations, and also with reference to reported Brookhaven Protein Database structures. It is the ultimate aim of this work to provide a method of examining protein structure that will complement existing major techniques. Peptide hydration can be explored using the ion chromatography cell as a reaction cell, and temperature variation here will allow thermodynamic measurements to be made of water association processes. In addition, it will be possible to study dynamics of structural change by trapping the ions for variable periods of time (and at various temperatures) prior to structural assessment.
Key Findings
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Potential use in non-academic contexts
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Impacts
Description This information can now be found on Gateway to Research (GtR) http://gtr.rcuk.ac.uk Summary Date Materialised
Sectors submitted by the Researcher
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Project URL:	http://www.barran.chem.ed.ac.uk/
Further Information:
Organisation Website:	http://www.ed.ac.uk