Article Abstract:
It has been possible to make a linear free-energy relationships (LFER) analysis of the gating reaction pathway of the muscle acetylcholine receptor. This research obtained a snapshot of a number of regions of the receptor at the transition state in terms of their approximate positions along the reaction coordinate. The fact that mutational effects can be ordered in an LFER is strong evidence that the mutations in question do not change the structure of the protein in extremely complicated ways. The systematic investigation of such mutant series can thus be seen as a very good analytical tool for looking in detail at allosteric-transition pathways.
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Article Abstract:
Single-molecule kinetic analysis is used to detect the transition state of gating conformational change and estimate relative timing of M2 motions in the [alpha]-subunit of the murine acetylcholine receptor. Results show that core of the channel serves both as a gate that regulates ion flow and as a hub that directs the propagation of gating isomerization through membrane domain of the acetylcholine receptor.
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Article Abstract:
The kinetics of transmitter binding and channel gating in single-channel currents from recombinant NR1/NR2A receptors are examined to show, that the synaptic response to trains of impulses is determined by the molecular reaction mechanism of the receptor. The molecular machinery of neurotransmitter receptors also determines the shape of the postsynaptic response to a single stimulus.
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