Long-range attraction and molecular rearrangements in receptor-ligand interactions

D. E. Leckband, J. N. Israelachvili, F. J. Schmitt, W. Knoll

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1419-1421
Number of pages3
JournalScience
Volume255
Issue number5050
DOIs
StatePublished - Jan 1 1992

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Ligands
Transition Temperature
Membranes
Proteins

ASJC Scopus subject areas

  • General

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Long-range attraction and molecular rearrangements in receptor-ligand interactions. / Leckband, D. E.; Israelachvili, J. N.; Schmitt, F. J.; Knoll, W.

In: Science, Vol. 255, No. 5050, 01.01.1992, p. 1419-1421.

Research output: Contribution to journalArticle

Leckband, D. E. ; Israelachvili, J. N. ; Schmitt, F. J. ; Knoll, W. / Long-range attraction and molecular rearrangements in receptor-ligand interactions. In: Science. 1992 ; Vol. 255, No. 5050. pp. 1419-1421.
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