title: Low-temperature neutron diffraction structures of N-glycoprotein linkage models and analogues: structure refinement and trifurcated hydrogen bonds.
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.
authors.affiliation: European Synchrotron Radiation Facility, BP220 Grenoble, France.
authors.forename: Gianluca
authors.initials: G
authors.lastname: Cioci
authors.forename: Amrita
authors.initials: A
authors.lastname: Srivastava
authors.forename: Duraikkannu
authors.initials: D
authors.lastname: Loganathan
authors.forename: Sax A
authors.initials: SA
authors.lastname: Mason
authors.forename: Serge
authors.initials: S
authors.lastname: Pérez
authors.forename: Anne
authors.initials: A
authors.lastname: Imberty
mesh_terms: D018360:Crystallography, X-Ray; D006023:Glycoproteins / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D033363:Neutron Diffraction; D011487:Protein Conformation; D013696:Temperature
chemical_list: D006023:Glycoproteins