Leckband D E, Israelachvili J N, Schmitt F J, Knoll W
Department of Chemical and Nuclear Engineering, University of California, Santa Barbara 93106.
Science. 1992 Mar 13;255(5050):1419-21. doi: 10.1126/science.1542789.
A surface force apparatus was used to measure a long-range attractive protein-ligand force at separations D less than 85 angstroms. This force may effectively "steer" ligand trajectories, resulting in a greater than 27-fold enhancement of the association rate. A much stronger specific attraction is measured at contact (D less than 4 angstroms). A sevenfold increase in intermembrane adhesion resulted from increased lateral mobility of the receptors and molecular rearrangements in membranes above the solid-fluid transition temperature.
使用表面力装置在小于85埃的间距D下测量长程吸引性蛋白质 - 配体力。这种力可有效地“引导”配体轨迹,导致缔合速率提高超过27倍。在接触时(D小于4埃)测量到更强的特异性吸引力。在高于固 - 液转变温度时,受体横向流动性增加以及膜内分子重排导致膜间粘附增加了七倍。