We propose the development of new and improved Nuclear Magnetic Resonance (NMR) techniques for the structural characterization and dynamic studies of small and medium-sized chemical molecules at natural abundance and also for large isotopically labelled \super 15\nosuper N y/0 \super 13\nosuper C/\super 2\nosuper H biomolecules, in particular proteins. We would like to apply our experience in the design of NMR methods, mainly based on the conventional principles and those described for heteronuclear cross-polarization in isotropic conditions. We are also interested to explore new spin-state-selective methodologies for the determination of scalar and residual dipolar coupling constants and to introduce robust NMR buiding blocks for a general use. In addition, we will focus our efforts on the implementation and the use of anisotropic media as a tool to obtain structural information of small molecules in aqueous and organic solvents from NMR studies. Thanks to the higher sensitivity achieved from a recently installed cryogenically cooled probe, we propose the extrapolation of these and other ideas to modern carbon-detected NMR experiments and also to mass-limited or low-solubility samples. Finally, we would like to take profit of the first hyphenated HPLC-NMR-SPE-MS system available in our country (to be installed in our NMR facility during 2006) that might allow us the use of the NMR spectroscopy to analyse complex mixtures and to expand our methodologies to NMR screening, molecular recognition and metabonomic applications in advantageous conditions.
|Effective start/end date||1/10/06 → 30/09/09|
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