完全经过几何优化的DFT/ONIOM三螺旋状原样结构,包含ProProGly,ProProAla,ProProDAla和ProProDSer三重体
Midas I-Hsien Tsai1, Yujia Xu, J J Dannenberg
1Department of Chemistry, City University of New York-Hunter College and The Graduate School, 695 Park Avenue, New York, NY 10021, USA.
Journal of the American Chemical Society
|October 13, 2005
概括
原蛋白的三环螺旋稳定性受到氨基酸突变的影响. 用D-氨基酸取代甘氨酸,特别是D-氨酸,可以通过额外的键稳定原结构.
科学领域:
- 生物化学 生物化学
- 计算化学的计算化学
- 结构生物学 结构生物学
背景情况:
- 原蛋白的三重螺旋结构对其机械性能至关重要.
- 甘氨酸在原中的每三个位置都是必需的氨基酸.
- 甘氨酸的形性质影响其在原中的作用.
研究的目的:
- 研究特定氨基酸突变对原样三环螺旋稳定性的影响.
- 为了探索L-氨酸,D-氨酸和D-氨酸替代甘氨酸的效果.
- 了解这些突变对螺旋稳定的能量贡献.
主要方法:
- 进行了ONIOM DFT/AM1分子轨道计算.
- 分析了原样三环螺旋和组件链的优化几何形状.
- 计算了野生类型和突变结构之间的能量差异.
主要成果:
- 替代L-氨酸显著破坏了三环螺旋的稳定.
- D-氨酸的替代稍微稳定了三环螺旋.
- 由于额外的键,D-氨酸的替代大大稳定了三环螺旋.
结论:
- 氨基酸的形性质在原三环稳定性中起着关键作用.
- 特定的D-氨基酸替代物,如D-氨酸,可以通过新的相互作用来增强原蛋白的稳定性.
- 计算建模为原蛋白中氨基酸突变的结构和能量后果提供了见解.
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