Substitution of a hydrophobic residue alters the conformational stability of Shaker K+ channels during gating and assembly
McCormack K, Lin L, Sigworth F. Substitution of a hydrophobic residue alters the conformational stability of Shaker K+ channels during gating and assembly. Biophysical Journal 1993, 65: 1740-1748. PMID: 8274662, PMCID: PMC1225901, DOI: 10.1016/s0006-3495(93)81202-5.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiophysical PhenomenaBiophysicsDNA, ComplementaryDrosophilaDrug StabilityFemaleIon Channel GatingMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedOocytesPeptidesPotassium ChannelsProtein ConformationShaker Superfamily of Potassium ChannelsThermodynamicsXenopus laevisConceptsUncharged amino acid residuesLeucine heptad repeatWild-type subunitsPosition 370Large hydrophobic residuesAmino acid residuesSequence motifsConservative substitutionsHeptad repeatHydrophobic residuesVoltage-gated channelsLeucine residuesAcid residuesTertiary structureS4 segmentSpecific hydrophobic interactionsHydrophilic residuesResidue altersChannel subunitsInactivation gatingChannel complexSubunitsConformational stabilityConformational transitionResidues