Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone
Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone
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DOI：
10.1016/s0009-2614(02)02046-8
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发表时间：
2003-02-17
影响因子：
2.8
通讯作者：
Vivian, JT
中科院分区：
文献类型：
--
作者：
Callis, PR;Vivian, JT
蛋白质中色氨酸(Trp)荧光量子产率的令人困惑的变化是通过量子力学-分子动力学模拟自然产生的，其中Trp环到酰胺主链电荷转移(CT)最低状态的能量在13种蛋白质的16个Trp的动力学轨迹中被监测。高位CT态的能量、涨落和驰豫对蛋白质环境(局部电场)和旋转构象高度敏感，导致L-1(A)的荧光产额和寿命有很大的变化。(C)2003 Elsevier Science B.V.保留所有权利。
A reasonable basis for the puzzling variation of tryptophan (Trp) fluorescence quantum yields in proteins arises naturally through quantum mechanics-molecular dynamics simulations in which the energy of the lowest Trp ring-to-amide backbone charge transfer (CT) state is monitored during dynamics trajectories for 16 Trps in 13 proteins. The energy, fluctuations, and relaxation of the high lying CT state are highly sensitive to protein environment (local electric field) and rotamer conformation, leading to large variations in L-1(a) fluorescence yield and lifetime. (C) 2003 Elsevier Science B.V. All rights reserved.