title: Long-range attraction and molecular rearrangements in receptor-ligand interactions.
abstract: 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.
authors.affiliation: Department of Chemical and Nuclear Engineering, University of California, Santa Barbara 93106.
authors.forename: D E
authors.initials: DE
authors.lastname: Leckband
authors.forename: J N
authors.initials: JN
authors.lastname: Israelachvili
authors.forename: F J
authors.initials: FJ
authors.lastname: Schmitt
authors.forename: W
authors.initials: W
authors.lastname: Knoll
mesh_terms: 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
chemical_list: D001426:Bacterial Proteins; D008024:Ligands; D008051:Lipid Bilayers; D001710:Biotin; D019809:Streptavidin