| Abstract: | Nuclear magnetic resonance spectroscopy (NMR) has become the most frequently used technique for the investigation of the structure of biomacromolecules in solution. In particular, selective relaxation techniques have been used in the analysis of homonuclear dipolar connectivities (selective and biselective proton spin-lattice relaxation experiments) and heteronuclear couplings (selective {H} C-NOE, biselective carbon R1 experiments). An accurate determination of selected i-j internuclear distances has made it possible to identify the preferred solution structure. A different experimental technique based on two-dimensional NOE spectra has made it possible to define the complex network of dipolar interactions that exists in biomacromolecules and hence the conformational properties in solution. |
