The energy and work of a ligand-gated ion channel.

ABSTRACT: Ligand-gated ion channels are allosteric membrane proteins that isomerize between C(losed) and O(pen) conformations. A difference in affinity for ligands in the two states influences the C↔O "gating" equilibrium constant. The energies associated with adult-type mouse neuromuscular nicotinic acetylcholine receptor (AChR) channel gating have been measured by using single-channel electrophysiology. Without ligands, the free energy, enthalpy and entropy of gating are ΔG0=+8.4, ΔH0=+10.9 and TΔS0=+2.5kcal/mol (-100mV, 23°C). Many mutations throughout the protein change ΔG0, including natural ones that cause disease. Agonists and most mutations change approximately independently the ground-state energy difference; thus, it is possible to forecast and engineer AChR responses simply by combining p

SUBMITTER: Auerbach A 

PROVIDER: S-EPMC4407511 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature