2020
Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations
Hoogerheide D, Rostovtseva T, Jacobs D, Gurnev P, Bezrukov S. Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations. ACS Nano 2020, 15: 989-1001. PMID: 33369404, PMCID: PMC9019845, DOI: 10.1021/acsnano.0c07672.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelMembrane surfaceSingle-molecule levelSame membrane surfaceIndividual proteinsAnion channelNeuronal proteinsLipid membranesBinding conformationsLipid surfaceLipid compositionProteinΑ-synucleinMembraneConformationOrders of magnitudeSurfaceUnbindingMitochondriaBindsObserved distributionNanoporesMoleculesΑSynTraps
2017
Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes
Hoogerheide D, Noskov S, Jacobs D, Bergdoll L, Silin V, Worcester D, Abramson J, Nanda H, Rostovtseva T, Bezrukov S. Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e3622-e3631. PMID: 28420794, PMCID: PMC5422764, DOI: 10.1073/pnas.1619806114.Peer-Reviewed Original ResearchConceptsMitochondrial outer membraneMitochondrial membraneOuter membraneDimeric tubulinPeripheral membrane proteinsMembrane-binding domainOuter mitochondrial membraneDomain of tubulinIntegral proteinsMembrane proteinsCytosolic proteinsPhysiological roleHelix H10TubulinLipid headgroupsProteinComplex mechanismsMembranePeripheral bindingStructural featuresEssential stepCytoskeletonElectrochemical impedance spectroscopyMitochondriaDomain