London E
Mol Cell Biochem. 1982 Jun 25;45(3):181-8. doi: 10.1007/BF00230086.
Fluorescence quenching is the loss of fluorescence intensity which is observed when a fluorescent molecule or group interacts with another molecule or group, called the quencher. By use of tryptophan residues of proteins, together with specific probe molecules, quenching can be applied to problems of biological and model membrane structure. Quenching interactions are short range (less than 50 A) so that structure on the scale of molecular dimensions can be examined. This review summarizes the recent applications of fluorescence quenching by spin (nitroxide)-labeled molecules to problems of membrane structure, including determination of the distance of membrane-bound molecules from the membrane surface, the strength of lipid-protein interactions and the strength of protein-protein interactions within membranes. The unique advantages and the limitations of this powerful method are examined.
荧光猝灭是指当荧光分子或基团与另一个分子或基团（称为猝灭剂）相互作用时观察到的荧光强度损失。通过利用蛋白质的色氨酸残基以及特定的探针分子，猝灭可应用于生物膜和模型膜结构问题的研究。猝灭相互作用的范围较短（小于50埃），因此可以研究分子尺寸尺度上的结构。本文综述了自旋（氮氧化物）标记分子荧光猝灭在膜结构问题上的最新应用，包括确定膜结合分子与膜表面的距离、脂-蛋白相互作用的强度以及膜内蛋白-蛋白相互作用的强度。同时考察了这种强大方法的独特优势和局限性。
