Ligand-receptor interactions
- 1 January 1999
- journal article
- review article
- Published by IOP Publishing in Reports on Progress in Physics
- Vol. 62 (6), 921-968
- https://doi.org/10.1088/0034-4885/62/6/202
Abstract
The formation and dissociation of specific noncovalent interactions between a variety of macromolecules play a crucial role in the function of biological system's. During the last few years, three main lines of research led to a dramatic improvement of our understanding of these important phenomena. First, a combination of genetic engineering and x-ray crystallography made available a simultaneous knowledge of the precise structure and affinity of series or related ligand-receptor systems differing by a few well-defined atoms. Second, improvement of computer power and simulation techniques allowed an extended exploration of the interaction of realistic macromolecules. Third, simultaneous development of a variety of techniques based on atomic force microscopy, hydrodynamic flow, biomembrane probes, optical tweezers, magnetic fields or flexible transducers yielded direct experimental information of the behaviour of single ligand-receptor bonds. At the same time, investigation of well-defined cellular models raised the interest of biologists to the kinetic and mechanical properties of cell membrane receptors. The aim of this review is to give a description of these advances that have benefited from a largely multidisciplinary approach.Keywords
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This publication has 166 references indexed in Scilit:
- Scanning Force Microscopy of the Interaction Events between a Single Molecule of Heavy Meromyosin and ActinBiochemical and Biophysical Research Communications, 1997
- Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesivenessNature, 1997
- Measuring the Lifetime of Bonds Made between Surface-linked MoleculesJournal of Biological Chemistry, 1995
- Structure of an Antibody–Lysozyme Complex Unexpected Effect of a Conservative MutationJournal of Molecular Biology, 1995
- Crystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interfaceJournal of Molecular Biology, 1992
- Solvation energy in protein folding and bindingNature, 1986
- Comparison of simple potential functions for simulating liquid waterThe Journal of Chemical Physics, 1983
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983
- Electron microscopy of an antibody-hapten complexJournal of Molecular Biology, 1967
- ber die Stabilit t und Aufladung der AerosoleThe European Physical Journal A, 1934