Multiple-Quantum NMR Spectroscopy: Detection of Slow Dynamics
Interference effects between two different spin-relaxation mechanisms that are quantified by measurements of the so-called “cross-correlated” relaxation have generated a lot of interest in the past several years (Frueh 2002). These studies provide information on protein dynamics at atomic resolution, including detailed insight into local motional anisotropy on the fast, ps–ns timescale complementing data obtained from traditional “auto-correlated” R1, R2 and NOE measurements (Cavanagh et al. 2007). In addition, valuable structural information that is very difficult, often impossible, to obtain from conventional measurements can be extracted from cross-correlated relaxation effects. These include backbone dihedral angles in proteins and sugar puckers in nucleic acids which can be incorporated as additional constraints into standard structure calculation and refinement protocols increasing the precision and accuracy of biomolecular structures...
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