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林和甘氨酸残留物对多链中循环形成的动力学和障碍物的影响
Florian Krieger1, Andreas Möglich, Thomas Kiefhaber
1Division of Biophysical Chemistry, Biozentrum der Universität Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
Journal of the American Chemical Society
|March 10, 2005
概括
甘氨酸和氨酸残留物影响蛋白质折叠的动态. Cis prolyl 键加速短环形成,而甘氨酸和跨 prolyl 键改变了这些关键蛋白质结构的激活能量.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 计算生物学 计算生物学
背景情况:
- 甘氨酸和氨酸残留物在蛋白质轮回和循环结构中很常见.
- 这些残留物被认为对折叠过程中早期蛋白质链紧缩至关重要.
研究的目的:
- 为了研究甘氨酸和氨酸对非结构性多的链内环形成动态的影响.
- 了解cis和trans prolyl键在循环形成动力学中的作用.
主要方法:
- 在各种非结构化的多链中模拟链内循环的形成.
- 对循环形成时间常数和激活能量的分析.
- 含有proline的的全原子模拟,以检查结构空间和变化.
主要成果:
- 环的形成在转烯键周围较慢,而在甘氨酸残留周围更快.
- 短循环 (2-10个残留物) 在cis prolyl键 (6 ns时间常数) 周围形成最快.
- 甘氨酸和转普罗利尔键通过激活能量影响循环形成,而cis普罗利尔键利用更高的预指数因子和受限的结构空间.
结论:
- 甘氨酸和氨酸残留物显著影响聚酸中短环形成 (2-10残留物) 的动态.
- 与trans异构体相比,cis prolyl异构体的受限构造空间可以促进更快的短环形成.
- 这些发现突出了甘氨酸和氨酸在蛋白质折叠中的特定作用,特别是对于原生蛋白质中功能相关的短环.
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