Dipartimento di Scienze e Tecnologie Chimiche, University of Rome Tor Vergata, via della Ricerca Scientifica 1, Rome, Italy.
Curr Opin Struct Biol. 2010 Apr;20(2):155-61. doi: 10.1016/j.sbi.2010.01.001. Epub 2010 Jan 29.
The state-of-the-art of theoretical-computational modelling of infrared (IR) spectra in peptides and proteins is able to reproduce the main spectral features involved in the secondary-structure organisation. The results so far collected, clearly show that the complexity of the atomic processes inherent to the IR spectra makes the often used empirical secondary-structure/frequency correlations inaccurate and possibly misleading. The use of extended configurational sampling as provided by, for example, molecular dynamics simulations and of a physically coherent treatment of both the quantum degrees of freedom and their coupling with the semiclassical atomic motions, promises to open the way to interpret and predict IR temperature-dependent and time-dependent spectral signals, in particular for the study of folding/unfolding transitions.
红外（IR）光谱在肽和蛋白质中的理论计算建模的最新进展能够再现与二级结构组织相关的主要光谱特征。迄今为止收集的结果清楚地表明，IR 光谱中固有的原子过程的复杂性使得常用的经验性二级结构/频率相关性不准确，并且可能具有误导性。例如，通过分子动力学模拟提供的扩展构型采样，以及对量子自由度及其与半经典原子运动的耦合的物理一致处理，有望为解释和预测 IR 随温度和时间变化的光谱信号开辟道路，特别是用于研究折叠/去折叠转变。
