LONG-RANGE ATTRACTION AND MOLECULAR-REARRANGEMENTS IN RECEPTOR-LIGAND INTERACTIONS

被引：122

作者：

LECKBAND, DE ^{[1
]}

ISRAELACHVILI, JN ^{[1
]}

SCHMITT, FJ ^{[1
]}

KNOLL, W ^{[1
]}

机构：

[1] MAX PLANCK INST POLYMER RES,W-6500 MAINZ,GERMANY

来源：

SCIENCE | 1992年 / 255卷 / 5050期

关键词：

D O I：

10.1126/science.1542789

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A surface force apparatus was used to measure a long-range attractive protein-ligand force at separations D < 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 < 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.

引用

页码：1419 / 1421

页数：3

共 24 条

[1] SIMULATION OF THE DIFFUSION-CONTROLLED REACTION BETWEEN SUPEROXIDE AND SUPEROXIDE-DISMUTASE .1. SIMPLE-MODELS [J].