Low-temperature neutron diffraction structures of N-glycoprotein linkage models and analogues: structure refinement and trifurcated hydrogen bonds |
| |
Authors: | Cioci Gianluca Srivastava Amrita Loganathan Duraikkannu Mason Sax A Pérez Serge Imberty Anne |
| |
Affiliation: | European Synchrotron Radiation Facility, BP220 Grenoble, France. |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |