Low-temperature neutron diffraction structures of N-glycoprotein linkage models and analogues: structure refinement and trifurcated hydrogen bonds.
J Am Chem Soc
; 133(26): 10042-5, 2011 Jul 06.
Article
en En
| MEDLINE
| ID: mdl-21648949
The biological addition of oligosaccharide moieties to asparagine residues of N-glycoproteins influences the properties and bioactivities of these macromolecules. The low-temperature neutron crystal structures of three N-glycoprotein linkage models and analogues provide accurate characterization of the three-dimensional structure of the conserved GlcNAc-Asn linkage. These first crystal structures of N-acetylated carbohydrates obtained by neutron diffraction provide high-resolution geometrical parameters that can be used for force-field parametrization and subsequent molecular dynamics simulation of N-glycoproteins. The correct localization of hydrogen atoms demonstrates the occurrence of trifurcated hydrogen bonds and hydrophobic contacts.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Temperatura
/
Glicoproteínas
/
Difracción de Neutrones
Idioma:
En
Revista:
J Am Chem Soc
Año:
2011
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos