High-resolution solid-state NMR structure of alanyl-prolyl-glycine.
J Magn Reson
; 200(1): 95-100, 2009 Sep.
Article
en En
| MEDLINE
| ID: mdl-19596601
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).
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Oligopéptidos
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Revista:
J Magn Reson
Asunto de la revista:
DIAGNOSTICO POR IMAGEM
Año:
2009
Tipo del documento:
Article
País de afiliación:
Estados Unidos