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Preparation and Reactivity of Gasless Nanostructured Energetic Materials
Published on: April 2, 2015
阿尔法螺旋在气相N端没有质子化
Robert Wieczorek1, J J Dannenberg
1Department of Chemistry, City University of New York-Hunter College and the Graduate School, 695 Park Avenue, New York, New York 10021, USA.
Journal of the American Chemical Society
|September 30, 2004
概括
阿尔法螺旋体的质子化最好发生在碳基末端,而不是氨基末端. 这一发现对于理解生物系统中的蛋白质结构和稳定性至关重要.
科学领域:
- 计算化学是一种计算化学.
- 生物物理学的生物物理.
- 蛋白质结构 蛋白质结构
背景情况:
- 阿尔法螺旋是蛋白质的基本二次结构.
- 了解不同条件下的α螺旋的行为对于蛋白质折叠和功能至关重要.
- 质子化部位可以显著影响和蛋白质的稳定性.
研究的目的:
- 为了研究短的阿尔法螺旋中的质子化首选位置.
- 为了确定质子化位置对α-螺旋稳定性和结构的影响.
- 探索这些发现对蛋白质捆中的α-螺旋体的影响.
主要方法:
- 使用密度函数理论 (DFT) 和AM1 ONIOM计算.
- 在计算中使用了B3LY/D95**基础集.
- 这项研究重点研究了与N = 14和17的alaN.
主要成果:
- 质子化最好发生在靠近碳酸末端的碳酸 (COOH) 和碳酸 (C=O) 基上.
- 在氨基末端的质子化导致局部螺旋解.
- 对于碳基终端质子化的偏好随着长度 (N) 的增加而增加.
- 化有利于N质子结构,但加剧了解.
结论:
- 阿尔法螺旋体的碳基末端比氨基末端更容易受到质子化的影响.
- 局部螺旋解与N端质子化有关.
- 这些发现表明,由于水分受限,蛋白质捆中的α螺旋体末端的C=O组可能很容易被质子化.
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