Back to Search
Start Over
Low-Temperature Neutron Diffraction Structures of N-Glycoprotein Linkage Models and Analogues: Structure Refinement and Trifurcated Hydrogen Bonds.
- Source :
-
Journal of the American Chemical Society . 7/6/2011, Vol. 133 Issue 26, p10042-10045. 4p. - Publication Year :
- 2011
-
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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00027863
- Volume :
- 133
- Issue :
- 26
- Database :
- Academic Search Index
- Journal :
- Journal of the American Chemical Society
- Publication Type :
- Academic Journal
- Accession number :
- 63149617
- Full Text :
- https://doi.org/10.1021/ja203239j