证明了蛋白质中不寻常的N-H··N键的证据
Ramkrishna Adhikary1, Jörg Zimmermann, Jian Liu
1Department of Chemistry, The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.
Journal of the American Chemical Society
|September 17, 2014
概括
以前被忽视的蛋白质胺基相互作用被证实是键. 这些键在蛋白质折叠,结构和功能中起着至关重要的作用.
科学领域:
- 生物化学 生物化学
- 结构生物学 结构生物学
- 频谱学是一种光谱学.
背景情况:
- 蛋白质含有大量的残留物,这些残留物通过胺N-H和前面残留物中的胺N之间的相互作用而稳定.
- 这些稳定相互作用的性质作为键仍然不完全理解.
研究的目的:
- 为了研究特定的蛋白质残留相互作用是否构成键.
- 阐明这些相互作用在蛋白质结构和功能中的作用.
主要方法:
- 红外 (红外) 拉伸频率的表征,使得化的变种和蛋白质.
- 密度函数理论 (DFT) 计算来分析电子相互作用.
主要成果:
- 减值的CδD2拉伸频率表明与Ni电子密度的超合.
- 质子化或Ni+1-H···Ni相互作用形成破坏了超合,导致C-D吸收的蓝色转移.
- DFT计算证实了IR数据,证实了Ni+1-H···Ni相互作用作为键.
结论:
- 蛋白质内的Ni+1-H···Ni相互作用以键为特征.
- 这些键可能会对蛋白质的折叠,稳定性和整体功能做出重大贡献.
- 这一发现突显了蛋白质结构生物学以前被低估的方面.
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