对原三环螺旋稳定性的cis-trans proline 异构化影响是有限的
1Department of Chemistry, Virginia Tech, Blacksburg, Virginia 24061, USA.
Journal of the American Chemical Society
|September 4, 2009
概括
在原中限制cis-trans proline异构化显著降低了三环螺旋稳定性. 这表明单个的烯异构化对原体的影响最小,但对原体的累积影响可能很大.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 类化学 类化学
背景情况:
- 原三环螺旋的稳定性对于连接组织至关重要.
- 烯异构化是影响形状的已知因素.
- 了解影响原蛋白稳定性的因素对于生物医学应用至关重要.
研究的目的:
- 为了研究受限制的cis-trans proline异构化对原三环螺旋稳定性的影响.
- 量化林异构化对总体原体结构的贡献.
- 为了比较改性与天然原蛋白的稳定性.
主要方法:
- 一个含有Pro-trans-Pro基异的宿主-客人的合成.
- 测量化温度 (T(m)) 以评估的稳定性.
- 稳定性数据与先前报告的含蛋白的稳定性数据的比较.
主要成果:
- 与对照组相比,Pro-trans-Pro基异类呈现了53.6°C较低的T(m).
- 这种修改后的比Pro-trans-Gly同位素更不稳定.
- 稳定性低于Gly-trans-Pro异类,突出显示了键的重要性.
结论:
- 单一的cis-trans proline 异构对原蛋白三环螺旋稳定性的影响有限.
- 在原的高氨基酸含量中,累积的异构化效应可能是显著的.
- 连锁骨干间的键是原三环稳定的主要驱动因素.
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