3-基林残留物对原蛋白稳定性的影响
Cara L Jenkins1, Lynn E Bretscher, Ilia A Guzei
1Contribution from the Department of Chemistry and Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Journal of the American Chemical Society
|June 6, 2003
概括
这项研究显示,3-基-l-proline (3-Hyp) 可以破坏原三重螺旋的稳定,与4-基-l-proline (4-Hyp) 不同. 它在原序列中的位置显著影响了这种对蛋白质稳定性的破坏效应.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 生物物理学的生物物理.
背景情况:
- 原蛋白是一种纤维蛋白,对结缔组织至关重要,具有三螺旋结构,重复氨基酸序列.
- 4R-基-l-proline (4-Hyp) 增强了原三环螺旋的稳定性.
- 3(S) - 基-l-proline (3-Hyp) 对原体稳定性的影响基本上是未知的.
研究的目的:
- 为了研究3-基-l-proline (3-Hyp) 对原体三螺旋稳定性的影响.
- 为了比较3-Hyp在原蛋白序列中的自然 (Xaa) 和非自然 (Yaa) 位置的影响.
主要方法:
- 合成两种宿主-客人,在不同位置结合3-Hyp.
- 对这些合成的结构稳定性的分析.
主要成果:
- 与proline相比,3-Hyp合成的两种都显示出减少了三螺旋稳定性.
- 在自然的Xaa位置中的3-Hyp通过削弱链间的键引起了轻微的不稳定.
- 在非自然的Yaa位置的3-Hyp导致了由于pyrrolidine环和硬质碰撞的显著不稳定.
结论:
- 与4-Hyp相比,3-Hyp对原三环螺旋稳定性有明显的影响.
- 3-Hyp (Xaa vs Yaa) 的位置决定了它对原蛋白稳定性的影响.
- 自然原蛋白序列可能会避免3-Hyp的Yaa位置以保持结构完整性.
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