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首页> 外文期刊>Journal of Carbohydrate Chemistry >X-Ray Crystallographic Investigation of Fully Acetylated N-(2-Deoxy-2-Acetamido-β-D-Glucopyranosyl)Alkanamides as N-Glycoprotein Linkage Region Analogs
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X-Ray Crystallographic Investigation of Fully Acetylated N-(2-Deoxy-2-Acetamido-β-D-Glucopyranosyl)Alkanamides as N-Glycoprotein Linkage Region Analogs

机译:X射线晶体学的完全乙酰化的N-(2-脱氧-2-乙酰氨基-β-D-Glucopyranosyl)烷酰胺作为N​​-糖蛋白链接区类似物。

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摘要

To understand the structural significance of the linkage region of N-glycoproteins, three title sugar amides have been prepared as analogs and their molecular assembly and crystal structures have been solved to explore the effect of acetyl protection and aglycon variation on the conformation, particularly of the N-glycosidic linkage. Comparative analysis of these structures with those of free sugar amides reported earlier showed that conformation of the amido aglycon moiety is not altered significantly by the masking of hydroxyl groups in the form of acetate. The bifurcated antiparallel pattern involving N‒H…O and C‒H…O hydrogen bonds, a hallmark of the N-glycoprotein models GlcNAcβNHAc and GlcNAcβAsn, is absent in all of the fully protected title alkanamides. The asymmetric unit of the tri-O-acetylated GlcNAcβNHAc contains two different conformations, in one of which the double-pillared hydrogen bond network involving C1 and C2 acetamido groups is antiparallel, while it is parallel in the other. The co-occurrence of a molecular assembly motif—a double-pillared parallel and antiparallel hydrogen bonding pattern—is hitherto unknown in the crystal structures of N-glycoprotein linkage region models and analogs.View full textDownload full textKeywords N-Glycoprotein, Linkage region, Analogs, X-ray, Molecular assemblyRelated var addthis_config = { ui_cobrand: "Taylor & Francis Online", services_compact: "citeulike,netvibes,twitter,technorati,delicious,linkedin,facebook,stumbleupon,digg,google,more", pubid: "ra-4dff56cd6bb1830b" }; Add to shortlist Link Permalink http://dx.doi.org/10.1080/07328303.2011.631237
机译:为了解N-糖蛋白连接区的结构重要性,已制备了三种标题糖酰胺作为类似物,并已解决了它们的分子组装和晶体结构,以探讨乙酰基保护和糖苷配基变异对构象的影响,特别是对蛋白的构象。 N-糖苷键。这些结构与较早报道的游离糖酰胺结构的比较分析表明,酰胺基糖苷配基部分的构象不会被乙酸盐形式的羟基掩盖而显着改变。 N糖蛋白模型GlcNAcβNHAc和GlcNAcβAsn的标志,涉及N'HαO和CâHαO氢键的分叉反平行模式在所有受完全保护的标题烷酰胺中均不存在。三O-乙酰化GlcNAcβNHAc的不对称单元包含两个不同的构象,其中一个涉及C1和C2乙酰氨基基团的双桩氢键网络是反平行的,而另一个则是平行的。迄今为止,在N-糖蛋白连接区域模型和类似物的晶体结构中,分子组装基序的共存(双柱平行和反平行氢键结合模式)是未知的。查看全文下载全文关键字N-糖蛋白,连接地区,类似物,X射线,分子组装相关的var addthis_config = {ui_cobrand:“泰勒和弗朗西斯在线”,servicescompact:“ citlikelike,netvibes,twitter,technorati,delicious,linkedin,facebook,stumbleupon,digg,google,更多”,pubid :“ ra-4dff56cd6bb1830b”};添加到候选列表链接永久链接http://dx.doi.org/10.1080/07328303.2011.631237

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