气相中的二次结构:N链 glycoproteins 的共识图案
Emilio J Cocinero1, E Cristina Stanca-Kaposta, David P Gamblin
1Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.
Journal of the American Chemical Society
|January 1, 2009
概括
二级结构影响N-链接糖蛋白中的NXS/T序列. 气相光谱和计算揭示了不同的构造,提供了对酶性糖化酶的洞察力.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 计算化学计算化学
背景情况:
- 与N结合的糖化对蛋白质功能至关重要.
- 共识序列NXS/T在N链 glycoproteins中保持一致.
- 本质二次结构在序列选择中的作用受到辩论.
研究的目的:
- 研究模拟NXS/T序列的的内在二次结构.
- 确定二级结构如何影响糖化位点的选择.
- 为了探索形和酶性糖基化之间的关系.
主要方法:
- 气相中的红外激光离子浸泡光谱.
- 开始和密度函数理论计算.
- 对封闭的寡类 (Ac-NGS-NHBn,Ac-QGS-NHBn,Ac-NPS-NHBn) 的分析.
主要成果:
- NGS采用S形形状,与溶液相Ax转不同.
- QGS 具有更强键的更刚性结构.
- NPS形成一个Asx转和一个C(10) β转,类似于晶体结构.
- 形状差异与侧链相互作用和潜在反应性相关.
结论:
- 内在的二次结构在确定共识序列方面发挥着重要作用.
- 由于环境因素,气相形状与溶液和晶体结构不同.
- 结构约束为阿斯巴拉金的酶性糖化提供了洞察力.
相关概念视频
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