Vibrational Echo Studies of Protein Dynamics.
Vibrational Echo Studies of Protein Dynamics.
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DOI：
10.1103/physrevlett.77.1648
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发表时间：
1996-08
影响因子：
8.6
通讯作者：
C. Rella;A. Kwok;K. Rector;J. R. Hill;H. A. Schwettman;D. Dlott;M. Fayer
中科院分区：
文献类型：
--
作者：
C. Rella;A. Kwok;K. Rector;J. R. Hill;H. A. Schwettman;D. Dlott;M. Fayer
第一皮秒红外振动回波实验上的蛋白质，肌红蛋白-CO，进行了说明。实验在60至300 K的温度范围内进行，使用调谐至1945 cm-1的中红外自由电子激光器。在185 K以下，纯失相T2 * 表现出幂律温度依赖性T1.3.这种行为让人想起与低温玻璃（< 5 K）的性质相关的行为，但是在这里在高得多的温度下观察到。在溶剂玻璃化转变温度以上，T2 * 呈指数激活.
The first picosecond infrared vibrational echo experiments on a protein, myoglobin-CO, are described. The experiments were performed at temperatures ranging from 60 to 300 K with a midinfrared free electron laser tuned to 1945 cm− 1. Below∼ 185 K, the pure dephasing, T 2*, displays a power law temperature dependence, T 1.3. This behavior is reminiscent of that associated with the properties of low temperature glasses (< 5 K) but is observed here at much higher temperatures. Above the solvent glass transition temperature, T 2* is exponentially activated.