caa a22 4500 477082998 CHVBK 20180405111455.0 cr unu---uuuuu 170330e19961201xx s 000 0 eng 10.1007/BF01952106 doi (NATIONALLICENCE)springer-10.1007/BF01952106 Allosteric proteins after thirty years: The binding and state functions of the neuronal α 7 nicotinic acetylcholine receptors [Elektronische Daten] [S. Edelstein, J. Changeux] A key statement of the 1965 Monod-Wyman-Changeux (MWC) model for allosteric proteins concerns the distinction between the ligand-binding function ( $$\bar Y$$ ) and the relevant state function ( $$\bar R$$ ). Sequential models predict overlapping behavior of the two functions. In contrast, a straightforward experimental consequence of the MWC model is that for an oligomeric protein the parameters which characterize the two functions should differ significantly. Two situations, where $$\bar R > \bar Y$$ and the system ishyper-responsive or where $$\bar R< \bar Y$$ and the system ishypo-responsive, have been encountered. Indeed, the hyper-responsive pattern was first observed for the enzyme aspartate transcarbamoylase, by comparing $$\bar Y$$ with $$\bar R$$ monitored by a change in sedimentation. Extensions of the theory to ligand-gated channels led to the suggestion that, on the one hand, hyper-responsive properties also occur with high-affinity mutants. On the other hand, native channels of the acetylcholine neuronalα7 receptor and low-affinity mutants of the glycine receptor can be interpreted in terms of the hypo-responsive pattern. For the ligand-gated channels, whereas $$\bar R$$ is detected directly by ion flux, ligand binding has rarely been measured and the formation of desensitized states may complicate the analysis. However, stochastic models incorporating both binding and channel opening for single molecules predict differences that should be measurable with new experimental approaches, particularly fluorescence correlation spectroscopy. Birkhäuser Verlag, 1996 Allosteric proteins nationallicence MWC model nationallicence ligand-gated channels nationallicence neuronal nicotinic acetylcholine receptors nationallicence stochastic models nationallicence Edelstein S. Département de Biochimie, Université de Genève, 30, quai Ernest-Ansermet, CH-1211, Genève 4, (Switzerland) aut Changeux J. Neurobiologie Moléculaire, Institut Pasteur, Paris, (France) aut Experientia Birkhäuser-Verlag 52/12(1996-12-01), 1083-1090 0014-4754 52:12<1083 1996 52 18 https://doi.org/10.1007/BF01952106 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01952106 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Edelstein S. Département de Biochimie, Université de Genève, 30, quai Ernest-Ansermet, CH-1211, Genève 4, (Switzerland) aut NATIONALLICENCE 700 1- Changeux J. Neurobiologie Moléculaire, Institut Pasteur, Paris, (France) aut NATIONALLICENCE 773 0- Experientia Birkhäuser-Verlag 52/12(1996-12-01), 1083-1090 0014-4754 52:12<1083 1996 52 18 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer