2024
DNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force
Chung M, Zhou K, Powell J, Lin C, Schwartz M. DNA-Based Molecular Clamp for Probing Protein Interactions and Structure under Force. ACS Nano 2024, 18: 27590-27596. PMID: 39344156, PMCID: PMC11518680, DOI: 10.1021/acsnano.4c08663.Peer-Reviewed Original ResearchConceptsTalin rod domainNegative-stain electron microscopyDouble-stranded DNADNA clampProtein functionRod domainCryptic sitesProtein interactionsMolecular clampCellular mechanotransductionStudy proteinsBiochemical studiesCell biologyAdult physiologyProtein conformationTalinProteinBiochemical scaleMultiple diseasesDNAARPC5LVinculinStructural analysisEmbryogenesisDNA-based devicesLipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow
Zhang Y, Lin C. Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow. Current Opinion In Cell Biology 2024, 88: 102377. PMID: 38823338, PMCID: PMC11193448, DOI: 10.1016/j.ceb.2024.102377.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMembrane tensionLipid transportNonvesicular lipid transportLipid transfer proteinsOrganelle biogenesisLipid transferMembrane proteinsMembrane domainsLipid homeostasisBiological functionsLipid flowMembrane protein densityTransfer proteinMembrane regionsProtein densityProteinMembraneLipidBiogenesisOrganelles
2022
Actuating tension-loaded DNA clamps drives membrane tubulation
Liu L, Xiong Q, Xie C, Pincet F, Lin C. Actuating tension-loaded DNA clamps drives membrane tubulation. Science Advances 2022, 8: eadd1830. PMID: 36223466, PMCID: PMC9555772, DOI: 10.1126/sciadv.add1830.Peer-Reviewed Original ResearchConceptsDNA clampMembrane tubulationMembrane dynamicsMembrane-remodeling eventsVesicle tubulationConformational changesSpatiotemporal controlDNA signalsCell membraneDNA nanostructuresTubulationMembrane deformationClosed stateOpen stateSelf-assembled DNA nanostructuresOrganismsProteinMembrane tubeArtificial systemsTube widthMembraneDynamics
2021
Sorting sub-150-nm liposomes of distinct sizes by DNA-brick-assisted centrifugation
Yang Y, Wu Z, Wang L, Zhou K, Xia K, Xiong Q, Liu L, Zhang Z, Chapman ER, Xiong Y, Melia TJ, Karatekin E, Gu H, Lin C. Sorting sub-150-nm liposomes of distinct sizes by DNA-brick-assisted centrifugation. Nature Chemistry 2021, 13: 335-342. PMID: 33785892, PMCID: PMC8049973, DOI: 10.1038/s41557-021-00667-5.Peer-Reviewed Original Research
2020
DNA-Origami-Based Fluorescence Brightness Standards for Convenient and Fast Protein Counting in Live Cells
Williams ND, Landajuela A, Kasula RK, Zhou W, Powell JT, Xi Z, Isaacs FJ, Berro J, Toomre D, Karatekin E, Lin C. DNA-Origami-Based Fluorescence Brightness Standards for Convenient and Fast Protein Counting in Live Cells. Nano Letters 2020, 20: 8890-8896. PMID: 33164530, PMCID: PMC7726105, DOI: 10.1021/acs.nanolett.0c03925.Peer-Reviewed Original ResearchConceptsCopies of proteinsBrightness standardsFluorescence microscopyProtein countingMammalian cellsFluorescent proteinCopy numberLive cellsConventional quantification techniquesBiological LaboratoryFluorescence microscopeProteinDNA origamiVersatile toolCellsBiologyCurrent quantification methodsCopiesOrganic dyes
2019
Quantification of Biomolecular Dynamics Inside Real and Synthetic Nuclear Pore Complexes Using Time-Resolved Atomic Force Microscopy
Stanley GJ, Akpinar B, Shen Q, Fisher PDE, Lusk CP, Lin C, Hoogenboom BW. Quantification of Biomolecular Dynamics Inside Real and Synthetic Nuclear Pore Complexes Using Time-Resolved Atomic Force Microscopy. ACS Nano 2019, 13: 7949-7956. PMID: 31241896, PMCID: PMC6660115, DOI: 10.1021/acsnano.9b02424.Peer-Reviewed Original ResearchConceptsNuclear pore complexAtomic force microscopyTransport barrierForce microscopyBiomolecular dynamicsPore complexNative nuclear pore complexesDynamics of biomoleculesNanometer length scaleDNA origami scaffoldMs temporal resolutionCollective transitionsMacromolecular trafficSelective gatewaySuch proteinsBiomolecular systemsOrigami scaffoldCohesive interactionsObserved dynamicsSuch experimentsTime scalesProteinBiological systemsLength scalesDrift correctionStiffness and Membrane Anchor Density Modulate DNA-Nanospring-Induced Vesicle Tubulation
Grome MW, Zhang Z, Lin C. Stiffness and Membrane Anchor Density Modulate DNA-Nanospring-Induced Vesicle Tubulation. ACS Applied Materials & Interfaces 2019, 11: 22987-22992. PMID: 31252462, PMCID: PMC6613048, DOI: 10.1021/acsami.9b05401.Peer-Reviewed Original ResearchConceptsVesicle tubulationMembrane-deforming proteinsDNA-based constructsMembrane anchorArtificial assemblageMembrane bindingSubcellular membranesDNA nanostructuresMembrane affinityTubulationLipid tubulesMembraneDNA nanotechnologyTunable architecturesPeptide densitySurface of liposomesProteinNanostructuresAssemblagesBindingAffinity
2018
Vesicle Tubulation with Self‐Assembling DNA Nanosprings
Grome MW, Zhang Z, Pincet F, Lin C. Vesicle Tubulation with Self‐Assembling DNA Nanosprings. Angewandte Chemie International Edition 2018, 57: 5330-5334. PMID: 29575478, PMCID: PMC5924453, DOI: 10.1002/anie.201800141.Peer-Reviewed Original ResearchConceptsMembrane-deforming proteinsDNA origami designMembrane tubulationMembrane tubulesMembrane curvatureMembrane surface coverageVesicle tubulationDNA structureLipid bilayersTubulationNanospringsTube morphologyIntricate interplayArtificial nanomachinesVesicle deformationSpherical vesiclesNanotechnologyMajor goalProteinDNAVesiclesNanomachinesBioengineeringDetergentsMorphology
2016
A Programmable DNA Origami Platform to Organize SNAREs for Membrane Fusion
Xu W, Nathwani B, Lin C, Wang J, Karatekin E, Pincet F, Shih W, Rothman JE. A Programmable DNA Origami Platform to Organize SNAREs for Membrane Fusion. Journal Of The American Chemical Society 2016, 138: 4439-4447. PMID: 26938705, PMCID: PMC4950518, DOI: 10.1021/jacs.5b13107.Peer-Reviewed Original ResearchConceptsMembrane fusionSoluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexCore molecular machineryMembrane fusion eventsProtein receptor complexMembrane fusion processMolecular machineryDNA origami platformTarget membraneAuxiliary proteinsIntracellular communicationDocking stepSingle-event levelReceptor complexLipid mixingSmall unilamellar vesiclesLipid bilayersSnareFundamental processesVesiclesUnilamellar vesiclesTraffickingMachineryProteinFusion
2015
Controlled Co-reconstitution of Multiple Membrane Proteins in Lipid Bilayer Nanodiscs Using DNA as a Scaffold
Raschle T, Lin C, Jungmann R, Shih WM, Wagner G. Controlled Co-reconstitution of Multiple Membrane Proteins in Lipid Bilayer Nanodiscs Using DNA as a Scaffold. ACS Chemical Biology 2015, 10: 2448-2454. PMID: 26356202, PMCID: PMC4769731, DOI: 10.1021/acschembio.5b00627.Peer-Reviewed Original ResearchConceptsMembrane protein complexesMultiple membrane proteinsVoltage-gated anion channelsMembrane proteinsProtein complexesHeterotrimeric membrane protein complexIndividual membrane proteinsLipid bilayer nanodiscsSingle nanodiscBilayer nanodiscsProtein aggregationMembrane environmentAnion channelNanodiscsProteinLipid bilayersModel systemProof of principleOligonucleotide sequencesComplementary oligonucleotide sequencesComplexesTemporary attachmentDNASequenceBilayers