Acuña A U, González-Rodríguez J, Lillo M P, Naqvi K R
Biophys Chem. 1987 Apr;26(1):63-70. doi: 10.1016/0301-4622(87)80008-x.
Human fibrinogen in solution was studied by monitoring the time-resolved depolarization of the fluorescence emitted by two spectroscopic labels of which the fluorescence lifetimes differ by an order of magnitude. Contrary to a long-held view, no evidence of molecular flexibility was found in the 10-1000 ns range. In addition, from the rate of the overall rotation, it is proposed that a prolate and symmetric ellipsoid of 47 X 10.5 nm may represent the time-averaged hydrodynamic size and shape of the protein in solution. This rigid and highly hydrated structure (4 g water/g protein) accommodates the latest nodular models obtained from electron microscopy, explains the singular hydrodynamics of fibrinogen and, apparently, it would perform the two main functions of the protein in haemostasis, blood coagulation and platelet aggregation, more efficiently than the flexible molecule.
通过监测两种光谱标记物发射荧光的时间分辨去极化来研究溶液中的人纤维蛋白原，这两种标记物的荧光寿命相差一个数量级。与长期以来的观点相反，在10 - 1000纳秒范围内未发现分子灵活性的证据。此外，根据整体旋转速率，有人提出一个长轴为47×10.5纳米的长形对称椭球体可能代表该蛋白质在溶液中的时间平均流体动力学尺寸和形状。这种刚性且高度水合的结构（每克蛋白质含4克水）与从电子显微镜获得的最新结节模型相符，解释了纤维蛋白原独特的流体动力学特性，而且显然，它在止血、血液凝固和血小板聚集过程中执行蛋白质的两种主要功能时，比柔性分子更高效。
