肌红蛋白-CO亚基结构和动态:多维振动回声和分子动态模拟
Kusai A Merchant1, W G Noid, Ryo Akiyama
1Department of Chemistry, Stanford University, Stanford, California 94305, USA.
Journal of the American Chemical Society
|November 6, 2003
概括
红外光谱学揭示了鱼碳一氧化蛋白 (MbCO) 中的histidine-64动态如何影响CO联体振动. 分子动力学模拟证实了这些发现,解释了振动脱相机制.
科学领域:
- 生物物理学的生物物理.
- 计算化学的计算化学
- 频谱学是一种光谱学.
背景情况:
- 碳一氧化球蛋白 (MbCO) 是研究蛋白质动力学和连接体相互作用的关键模型.
- 了解连接体的振动脱相提供了对蛋白质构造子状态的洞察.
研究的目的:
- 为了研究300 K的精油MbCO中CO联体的振动脱相动力学.
- 为了将实验光谱数据与分子动力学 (MD) 模拟相关联.
- 阐明histidine-64 (His64) 质子和动态在CO联体振动脱相中的作用.
主要方法:
- 带有光谱分辨率的红外刺激振动回声谱.
- 全原子分子动力学 (MD) 模拟.
- 对振动脱相动力学和蛋白质构造次态的分析.
主要成果:
- 碳化合物联体的实验脱相动力学与对质子化His64 (N(epsilon) -H的MD模拟一致.
- 两个MD形态子状态 (B(epsilon) 和R(epsilon)) 分别被分配到光谱子状态A(1) 和A(3).
- 他的64动态被确定为CO振动脱相的主要来源在A(3) 状态和A(1) 状态的重要因素.
结论:
- His64的质子化状态和动态在MbCO.CO中CO联体的振动脱相中发挥着至关重要的作用.
- 模拟MD准确地预测实验观测,验证模型.
- MbCO 的不同形态子状态表现出不同的脱相机制,受 His64 和溶剂相互作用的影响.
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