By a News Reporter-Staff News Editor at Science Letter -- New research on Proteins is the subject of a report. According to news reporting originating in Tamil Nadu, India, by NewsRx journalists, research stated, "N-Glycoprotein linkage region constituents namely 2-deoxy-2-acetamido-beta-D-glucopyranose (GlcNAc) and asparagine (Asn) are conserved among all eukaryotes. Earlier crystallographic studies on the linkage region conformation revealed that among all the models and analogs of the N-glycoprotein linkage region, Xyl beta NHAc showed maximum deviation in the phi(N) value as compared to the value reported for the model compound, GlcNAc beta NHAc."
The news reporters obtained a quote from the research from the Indian Institute of Technology, "In order to understand the effect of another pentopyranose, viz., arabinose, on the N-glycosidic torsion angles and molecular assembly, three arabinopyranosyl alkanamides were synthesized and their X-ray crystal structures elucidated. A comparative analysis of the N-glycosidic torsion, phi(N) of the three analogs revealed the greater rotational freedom around the C1-N1 bond as compared to the GlcNAc derivatives. Molecular assembly of propionamido and chloroacetamido derivatives is characterized by the presence of anti-parallel bilayers of the molecules. This unique molecular assembly is hitherto unknown in all other models and analogs of N-glycoprotein linkage region."
According to the news reporters, the research concluded: "This study reveals that N-glycosidic torsions are influenced by the glycan as well as molecular packing."
For more information on this research see: Synthesis and X-ray crystallographic investigation of N-(alpha-D-arabinopyranosyl)alkanamides as N-glycoprotein linkage region analogs. Carbohydrate Research, 2013;380():92-100. Carbohydrate Research can be contacted at: Elsevier Sci Ltd, The Boulevard, Langford Lane, Kidlington, Oxford OX5 1GB, Oxon, England. (Elsevier - www.elsevier.com; Carbohydrate Research - www.elsevier.com/wps/product/cws_home/424829)
Our news correspondents report that additional information may be obtained by contacting A. Srivastava, Indian Inst Technol, Sophisticated Analyt Instrumentat Facil, Madras 600036, Tamil Nadu, India. Additional authors for this research include B. Varghese and D. Loganathan (see also Proteins).
Keywords for this news article include: Asia, India, Tamil Nadu, Glycoproteins, Nanotechnology, Glycoconjugates, Molecular Assemblies, Emerging Technologies
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