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[资源] Chem.Soc.Rev. 最新综述:荧光共振能量转移和驱动蛋白分子

阿姆斯特丹自由大学（VU University Amsterdam）的 Erwin J.G. Peterman在Chemical Society Reviews上发表了荧光共振能量转移和驱动蛋白分子的综述。
Abstract：Förster Resonance Energy Transfer (FRET) is the phenomenon of non-radiative transfer of electronic excitations from a donor fluorophore to an acceptor, mediated by electronic dipole–dipole coupling. The transfer rate and, as a consequence, efficiency depend non-linearly on the distance between the donor and the acceptor. FRET efficiency can thus be used as an effective and accurate reporter of distance between two fluorophores and changes thereof. Over the last 50 years or so, FRET has been used as a spectroscopic ruler to measure conformations and conformational changes of biomolecules. More recently, FRET has been combined with microscopy, ultimately allowing measurement of FRET between a single donor and a single acceptor pair. In this review, we will explain the physical foundations of FRET and how FRET can be applied to biomolecules. We will highlight the power of the different FRET approaches by focusing on its application to the motor protein kinesin, which undergoes several conformational changes driven by enzymatic action, that ultimately result in unidirectional motion along microtubule filaments, driving active transport in the cell. Single-molecule and ensemble FRET studies of different aspects of kinesin have provided numerous insights into the complex chemomechanical mechanism of this fascinating protein.
荧光共振能量转移（FRET）是荧光供体到受体直接电子激发态的非辐射符合转移，通过电子偶极-偶极联接调节。因此，有效的转移速率取决于供体和受体直接的非线性距离。FRET的效率可以用作两个荧光基团距离和变化实际和精确的监控器。在过去的50年里，FRET已经被用作生物分子构造和构型变化的“光谱标尺”。而且最近，FRET和显微镜技术结合，最终测量单分子供体和单分子受体对直接的FRET效率。
在本文中，我们解释了FRET的物理基础，以及FRET技术如何应用于生物分子。在驱动蛋白分子应用方面，我们强调了不同FRET方法的差别，主要是由于酶催化活性导致的不同的构象变化，最终导致沿着微管细丝的单向性的运动，进而驱动细胞内的主动运输。不同方面的驱动蛋白的单分子和整体FRET研究为这一精妙蛋白质的复杂的化学机械机制提供了深刻见解。

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2014-01-05 19:41:06, 2.34 M