RTACQ4PSNMR

Ultrahigh resolution NMR tools for chemistry and structural biology

Coordinatore	more  Organization address address: OXFORD ROAD city: MANCHESTER postcode: M13 9PL contact info Titolo: Ms. Nome: Liz Cognome: Fay Email: send email Telefono: 441613000000 Fax: 441613000000
Nazionalità Coordinatore	Non specificata
Totale costo	221˙606 €
EC contributo	221˙606 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2013-IEF
Funding Scheme	MC
Anno di inizio	2014
Periodo (anno-mese-giorno)	2014-03-03   -   2016-03-02

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	THE UNIVERSITY OF MANCHESTER  Organization address address: OXFORD ROAD city: MANCHESTER postcode: M13 9PL contact info Titolo: Ms. Nome: Liz Cognome: Fay Email: send email Telefono: 441613000000 Fax: 441613000000	UK (MANCHESTER)	coordinator	221˙606.40

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 Obiettivo del progetto (Objective)

'Solution NMR spectroscopy is among the most important techniques in natural science, particularly for structural biology and organic chemistry research. Spectral resolution and sensitivity are the key parameters controlling access to structural information at the atomic level; at present it is resolution that limits the complexity of structural problem, whether chemical or biological, that NMR can be applied to. Multidimensional NMR has allowed huge strides to be made in studies of the 3D structure and dynamics of complex molecules, but in each dimension the multiplet structure caused by homonuclear couplings sets the resolution limit. Very recently, an improvement to one of the most widely-used and prototypical techniques, the HSQC experiment, has been published by the NMR methodology group at Manchester University headed by Gareth Morris and Mathias Nilsson. This uses for the first time suppression of homonuclear proton-proton couplings in real time during HSQC data acquisition, and results in a simultaneous improvement of a factor of two or more in both resolution and sensitivity, marking a significant breakthrough. Initial results confirm that the basic approach is viable in macromolecular systems, including proteins. Similar approaches should be applicable to a wide range of multidimensional techniques, and have the potential to increase significantly the structure-determining power of NMR. This project sets out plans for the development of a range of novel real-time acquisition methods, including for example improved 3D triple-resonance pulse sequences for protein backbone assignment, and exploiting synergies between real-time homonuclear decoupling and non-uniform data sampling methods to maximise the efficiency of structural studies of complex systems by NMR.'