Myoglobin-CO conformational substate dynamics: 2D vibrational echoes and MD simulations
Myoglobin-CO conformational substate dynamics: 2D vibrational echoes and MD simulations
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DOI：
10.1016/s0006-3495(02)75669-5
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发表时间：
2002-06-01
影响因子：
3.4
通讯作者：
Fayer, MD
中科院分区：
文献类型：
--
作者：
Merchant, KA;Thompson, DE;Fayer, MD
在一定温度范围内，对马心一氧化碳肌球蛋白(MbCO)在水中进行了二维红外振动回波。发现MbCO的A(1)和A(3)构象亚态随温度的变化具有不同的脱相速率。用298K下MbCO分子动力学模拟得到的频率-频率关联函数计算了振动回波衰减。计算的衰变与实验测量的衰变基本一致。2D振动回波探测蛋白质动力学，并提供可用于测试MbCO构象亚态结构指定的观察值。
Two-dimensional (2D) infrared vibrational echoes were performed on horse heart carbonmonoxymyoglobin (MbCO) in water over a range of temperatures. The A(1) and A(3) conformational substates of MbCO are found to have different dephasing rates with different temperature dependences. A frequency-frequency correlation function derived from molecular dynamics simulations on MbCO at 298 K is used to calculate the vibrational echo decay. The calculated decay shows substantial agreement with the experimentally measured decays. The 2D vibrational echo probes protein dynamics and provides an observable that can be used to test structural assignments for the MbCO conformational substates.