霍夫迈斯特离子与蛋白质的结合口袋之间的相互作用
Jerome M Fox1, Kyungtae Kang1, Woody Sherman2
1†Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, United States.
Journal of the American Chemical Society
|March 5, 2015
概括
霍夫迈斯特阳离子通过与辅助因子形成离子对或与疏水区域相互作用,与蛋白质口袋结合. 阳离子结合改变了蛋白质内的水结构,超越了最初的水化.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 物理化学 物理化学
背景情况:
- 霍夫迈斯特阳离子影响蛋白质的结构和功能.
- 了解离子-蛋白相互作用是生物过程的关键.
- 水在离子-蛋白结合中的作用是复杂的.
研究的目的:
- 调查霍夫迈斯特离子与人类碳酸无水酶II (HCAII) 的结合.
- 确定离子属性如何决定结合位置和强度.
- 检查阴离子结合对蛋白质内水结构的影响.
主要方法:
- 用X射线晶体学可视化离子-蛋白相互作用.
- 异热定位热量计用于量化结合热力学.
- 模拟分子动力学以研究水的重新排列.
主要成果:
- 阳离子与HCAII中的Zn2+) 辅因子形成内球离子对.
- 离子-Zn(2+) 的关联强度与离子脱水能量相关.
- 化物和化物与疏水区域结合;阴离子将水重组至8 Å.
结论:
- 弱水合的阳离子与补充的疏水口袋结合.
- 蛋白质中的离子诱导的水重组是广泛的.
- 霍夫迈斯特离子是多功能连接体,可以改变蛋白质的水分和电荷分布.
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