原蛋白的阿扎甘氨酸稳定性的结构基础
Alexander J Kasznel1, Yitao Zhang1, Yang Hai1
1Department of Chemistry and ‡Department of Bioengineering, University of Pennsylvania , Philadelphia, Pennsylvania 19104-6323, United States.
Journal of the American Chemical Society
|June 27, 2017
概括
通过增加热稳定性来稳定原蛋白. 这种涉及单个原子的修改增强了三环螺旋的稳定性,并为改善原蛋白性能提供了结构基础.
科学领域:
- 生物化学
- 结构生物学
- 类化学
背景情况:
- 原三螺旋的稳定性对它的功能至关重要.
- 糖氨酸残留物在原体中严格保存.
- 之前的研究表明,阿扎甘氨酸可以稳定原蛋白.
研究的目的:
- 研究含有阿金的原蛋白中的aza-glycine替代.
- 确定阿扎-甘氨酸稳定性的结构基础.
- 评估aza-glycine对原蛋白热稳定性的影响.
主要方法:
- 在蛋白中以阿扎甘氨酸替代.
- 热稳定性测量 (化温度)
- 原子分辨率的晶体结构的确定.
主要成果:
- 亚扎甘氨酸的替代增加了含有氨酸的化温度8.6°C.
- 一个原子分辨率的晶体结构为稳定提供了基础.
- 观察到骨结构的最小变化.
结论:
- 阿扎甘氨酸是稳定的一般策略.
- 单个原子的替代增强了三螺旋的稳定性.
- 这种修改为设计更稳定的原材料提供了途径.
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