title: High-resolution solid-state NMR structure of alanyl-prolyl-glycine.
abstract: 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 (13)C-(13)C distance constraints are extracted by fitting rotational resonance width (R(2)W) 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 (13)C-(13)C 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 (0.02A backbone RMSD using all 11 constraints).
authors: Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts, Institute of Technology, Cambridge, MA 02139, USA.
authors: Alexander B
authors: AB
authors: Barnes
authors: Loren B
authors: LB
authors: Andreas
authors: Matthias
authors: M
authors: Huber
authors: Ramesh
authors: R
authors: Ramachandran
authors: Patrick C A
authors: PC
authors: van der Wel
authors: Mikhail
authors: M
authors: Veshtort
authors: Robert G
authors: RG
authors: Griffin
authors: Manish A
authors: MA
authors: Mehta
mesh_terms: D002247:Carbon Isotopes; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015233:Models, Statistical; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D002247:Carbon Isotopes; D009842:Oligopeptides; C545237:alanyl-prolyl-glycine