Details of Grant 

EPSRC Reference:	GR/R96897/01
Title:	A new solid-state NMR experiment for the investigation of protein structures
Principal Investigator:	Duer, Professor M
Other Investigators:
Researcher Co-Investigators:
Project Partners:
Department:	Chemistry
Organisation:	University of Cambridge
Scheme:	Standard Research (Pre-FEC)
Starts:	01 April 2003	Ends:	31 March 2006	Value (£):	83,659
EPSRC Research Topic Classifications:	Analytical Science Chemical Biology Chemical Structure
EPSRC Industrial Sector Classifications:	No relevance to Underpinning Sectors
Related Grants:
Panel History:
Summary on Grant Application Form
The aim of this project is to develop and use a new solid-state NMR method for structure determination in proteins. The last few years have seen a huge increase in the use of solid-state NMR for protein structure determination. Where proteins can be crystallized into high quality single crystals, X-ray diffraction is still the method of choice for structure determination of such systems. However, in many cases, X-ray diffraction is still unable to provide detailed structural parameters, such as bond torsion angles along the protein backbone. In many other cases, it has so far proved impossible to form suitable single crystals of the protein under study. This is the case for instance, for solid, structural proteins, such as keratin, collagen and elastin which are inherently insoluble. For these proteins, and many others, solid-state NMR remains an invaluable tool in structure determination, and in particular for determining bond torsion angles along the protein backbone.In this project, we will develop a new solid-state NMR experiment involving 13C-14N triple quantum coherence for use in assessing protein backbone conformation. The aim of the experiment is to allow the measurement of the orientations of the 14N quadrupole coupling and 13C chemical shift anisotropy tensors relative to the 13C-14N vector. This in turn should give information on the torsion angle about the t 3C-14N bond.
Key Findings
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Organisation Website:	http://www.cam.ac.uk