High-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycine
We present a de novo high-resolution structure of the peptide Alanyl-Prolyl-Glycine using a combination of sensitive solid-state NMR techniques that each yield precise structural constraints. High-quality 13C–13C distance constraints are extracted by fitting rotational resonance width (R2W) experiments using Multimode Multipole Floquet Theory and experimental chemical shift anisotropy (CSA) orientations. In this strategy, a structure is first calculated using DANTE-REDOR and torsion angle measurements and the resulting relative CSA orientations are used as an input parameter in the 13C–13C distance calculations. Finally, a refined structure is calculated using all the constraints. We investigate the effect of different structural constraints on structure quality, as determined by comparison to the crystal structure and also self-consistency of the calculated structures. Inclusion of all or subsets of these constraints into CNS calculations resulted in high-quality structures (0.02 Å backbone RMSD using all 11 constraints).
Barnes, Alexander B., Loren B. Andreas, Matthias Huber, Ramesh Ramachandran, et al. 2009. "High-Resolution Solid-State NMR Structure of Alanyl-Prolyl-Glycine." Journal Of Magnetic Resonance 200(1): 95-100.
Journal of Magnetic Resonance
Chemistry and Biochemistry