• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Chemistry: A European journal >Chemical Synthesis of Glycoproteins with the Specific Installation of Gradient-Enriched ~(15)N-Labeled Amino Acids for Getting Insights into Glycoprotein Behavior
【24h】

Chemical Synthesis of Glycoproteins with the Specific Installation of Gradient-Enriched ~(15)N-Labeled Amino Acids for Getting Insights into Glycoprotein Behavior

机译：糖蛋白的化学合成具有梯度富含梯度〜（15）N-标记的氨基酸的特异性安装，用于对糖蛋白行为进行洞察

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Elucidating the effects of oligosaccharides on glycoprotein properties, such as local conformational changes, stability, and dynamics, has still been challenging. In this paper, a novel partial ~(15)N-labeling method for the amide backbone of a synthetic glycoprotein is proposed. Using solid-phase peptide synthesis (SPPS) and native chemical ligation (NCL), thirteen ~(15)N-labeled amino acids were inserted at specific positions of the protein backbone, while intentionally varying the enrichment of ~(15)N atoms. This idea discriminated even the same type of amino acid based on the intensities of ~1H-~(15)N HSQC signals, combined with classic homonuclear TOCSY and NOESY methods, thus allowing for understanding the dynamics of the local conformation of a synthetic homogeneous glycoprotein. Results suggested that the attachment of an oligosaccharide of either a bi-antennary complex-type or a high-mannose-type did not disturb protein conformation. However, T_1 values suggested that the oligosaccharide influenced dynamics at the local conformation. Temperature-varied circular dichroism (CD) spectra and T_1 values clearly indicated that oligosaccharides appeared to inhibit protein fluctuation or, in other words, stabilize protein structure. This insight into oligosaccharide behavior suggests some further effects on binding affinity between a glycoprotein and its receptor.
机译：阐明寡糖对糖蛋白性质的影响，例如局部构象变化，稳定性和动力学，仍然是挑战性的。本文提出了一种新的偏〜（15）N-标记方法，用于合成糖蛋白的酰胺骨干骨架。使用固相肽合成（SPP）和天然化学结扎（NCL），在蛋白质骨架的特定位置插入13〜（15）n标记的氨基酸，同时有意地改变〜（15）n原子的富集。这种想法甚至基于相同类型的氨基酸基于〜1H-〜（15）N HSQC信号的强度，与经典的同核TACSY和NOESY方法相结合，从而允许了解合成均匀糖蛋白的局部构象的动态。结果表明，二核复合型或高甘露糖型的寡糖的附着不干扰蛋白质构象。然而，T_1值表明寡糖影响了局部构象的动力学。温度变化的圆形二色性（CD）光谱和T_1值清楚地表明寡糖似乎抑制蛋白质波动或换句话说，稳定蛋白质结构。这种对寡糖行为的洞察力表明对糖蛋白及其受体之间的结合亲和力有一些进一步的影响。

著录项

相似文献

  • 外文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号