Schuler Benjamin, Eaton William A
Biochemisches Institut, Universität Zürich, Winterthurerstr. 190, 8057 Zürich, Switzerland.
Curr Opin Struct Biol. 2008 Feb;18(1):16-26. doi: 10.1016/j.sbi.2007.12.003. Epub 2008 Jan 24.
A complete understanding of a protein-folding mechanism requires description of the distribution of microscopic pathways that connect the folded and unfolded states. This distribution can, in principle, be described by computer simulations and theoretical models of protein folding, but is hidden in conventional experiments on large ensembles of molecules because only average properties are measured. A long-term goal of single-molecule fluorescence studies is to time-resolve the structural events as individual molecules make transitions between folded and unfolded states. Although such studies are still in their infancy, the work till now shows great promise and has already produced novel and important information on current issues in protein folding that has been impossible or difficult to obtain from ensemble measurements.
对蛋白质折叠机制的完整理解需要描述连接折叠态与未折叠态的微观路径分布。原则上，这种分布可以通过蛋白质折叠的计算机模拟和理论模型来描述，但在对大量分子集合进行的传统实验中却难以得知，因为测量的只是平均性质。单分子荧光研究的一个长期目标是在单个分子在折叠态和未折叠态之间转变时对结构事件进行时间分辨。尽管此类研究仍处于起步阶段，但迄今为止的工作显示出巨大的前景，并且已经产生了关于蛋白质折叠当前问题的新颖且重要的信息，这些信息从集合测量中是不可能或难以获得的。
