Novel Experimental Techniques in Nuclear Magnetic Resonance of Biomolecules

Project description:

A general goal of NMR studies of biomolecules is to obtain as accurate as possible data that can characterize the structure and/or dynamics of the studied system. A necessary first step in any NMR study is the resonance assignment. For this purpose, the methods that rely on through-bond interactions are preferable. Methods to allow complete resonance assignment of both proteins and nucleic acids have been developed by now. Today, the task is to improve the sensitivity and resolution of the methods to allow application to bimolecular systems of increasing complexity.
No matter how sophisticated assignment methods may be, the structure calculations relied up to recently mostly on restraints derived from NOE spectra that include only local interactions. Therefore, additional sources of structural constraints are being investigated such as residual dipolar couplings and structural dependence of either isotropic chemical shifts or chemical shift anisotropy. New efficient methods are therefore needed to measure small changes in spin-spin couplings induced by oriented media and to obtain accurate values of chemical shifts of as many nuclei in the molecule as possible.

Example of a pulse scheme for a two-dimensional NMR experiment

Figure 1: Example of a pulse scheme for a two-dimensional NMR experiment. The scheme shown is for the HCNC experiment proposed for establishing connectivities between H8 and C4 in the purine bases and between H6 and C2 in the pyrimidine bases of nucleic acids (Fiala et al. J. Biomol. NMR 2004 29: 477-490).


Design © oliver 2007