Long-range attraction and molecular rearrangements in receptor-ligand interactions.
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.
Leckband
D E
DE
Department of Chemical and Nuclear Engineering, University of California, Santa Barbara 93106.
Israelachvili
J N
JN
Schmitt
F J
FJ
Knoll
W
W
D001426:Bacterial Proteins / Q000378:metabolism; D001710:Biotin / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004563:Electrochemistry; D008024:Ligands; D008051:Lipid Bilayers; D008956:Models, Chemical; D011485:Protein Binding / Q000502:physiology*; D019809:Streptavidin
D001426:Bacterial Proteins; D008024:Ligands; D008051:Lipid Bilayers; D001710:Biotin; D019809:Streptavidin