2017
Single-molecule force spectroscopy of protein-membrane interactions
Ma L, Cai Y, Li Y, Jiao J, Wu Z, O'Shaughnessy B, De Camilli P, Karatekin E, Zhang Y. Single-molecule force spectroscopy of protein-membrane interactions. ELife 2017, 6: e30493. PMID: 29083305, PMCID: PMC5690283, DOI: 10.7554/elife.30493.Peer-Reviewed Original ResearchConceptsProtein-membrane interactionsC2 domainPlasma membraneMultiple C2 domainsSingle-molecule force spectroscopy approachSingle-molecule force spectroscopyOptical tweezersE-SytsUnprecedented spatiotemporal resolutionForce spectroscopyMembrane bindingMembrane fusionSingle proteinSynaptotagmin-1Biological processesEndoplasmic reticulumSpectroscopy approachLipid exchangeSynaptic vesiclesSynaptotagmin 2ProteinSilica beadsMechanical forcesHigh-resolution methodsSpatiotemporal resolution
2009
Closing the Loop on Protein-DNA Interactions: Interplay Between Shape and Flexibility in Nucleoprotein Assemblies Having Implications for Biological Regulation
Levene S, Zhang Y. Closing the Loop on Protein-DNA Interactions: Interplay Between Shape and Flexibility in Nucleoprotein Assemblies Having Implications for Biological Regulation. The IMA Volumes In Mathematics And Its Applications 2009, 150: 195-212. DOI: 10.1007/978-1-4419-0670-0_10.Peer-Reviewed Original ResearchDNA loop formationProtein-DNA interactionsProtein-binding sitesArchitectural proteinsGene repressionLoop formationGene regulationProtein domainsDNA replicationDNA loopsNucleoprotein assembliesBiological regulationLac repressorBiological processesBiological importanceConformational flexibilityProteinEssential mechanistic aspectsDNARegulationSingle moleculesRepressorMechanistic aspectsDistant sitesRepression