2015
Label-Free Biosensor Imaging on Photonic Crystal Surfaces
Zhuo Y, Cunningham B. Label-Free Biosensor Imaging on Photonic Crystal Surfaces. Sensors 2015, 15: 21613-21635. PMID: 26343684, PMCID: PMC4610529, DOI: 10.3390/s150921613.Peer-Reviewed Original ResearchMeSH KeywordsBiocompatible MaterialsBiosensing TechniquesEquipment DesignNanoparticlesPhotonsProtein BindingConceptsPhotonic crystal surfaceCrystal surfaceImaging detection instrumentMetal plasmonic nanoparticlesDielectric nanoparticlesPhotobleachable fluorescent dyesOptical scatteringDielectric permittivityNanostructure designSensing resolutionOperating principleSubstrate surfaceCytotoxic stainsOptical microscopyPlasmonic nanoparticlesBiomaterial interactionsMatrix surfaceBiomolecular layerDetection instrumentKinetic monitoringPhotonsLabel-freeNanoparticlesSurfaceNanoparticle contrast agents
2014
Protein-protein Binding Detection with Nanoparticle Photonic Crystal Enhanced Microscopy (NP-PCEM)* *Research supported by National Science Foundation
Zhuo Y, Tian L, Chen W, Yu H, Singamaneni S, Cunningham B. Protein-protein Binding Detection with Nanoparticle Photonic Crystal Enhanced Microscopy (NP-PCEM)* *Research supported by National Science Foundation. Annual International Conference Of The IEEE Engineering In Medicine And Biology Society (EMBC) 2014, 2014: 2069-2072. PMID: 25570391, DOI: 10.1109/embc.2014.6944023.Peer-Reviewed Original ResearchConceptsPhotonic crystalsLocalized surface plasmon resonance frequencyPC biosensorPhotonic crystal biosensorIndividual nanoparticlesSurface plasmon resonance frequencyPlasmon resonance frequencyResonance wavelengthExperimental demonstrationPresence of individual nanoparticlesBiosensing approachProtein-protein bindingBiosensorFunctionalized nanoparticlesNanoparticlesResonant frequencySurface adsorptionNanoparticle resolutionCrystalBinding detectionImaging approachResonanceFinite-differenceWavelength
2013
Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2
Sun J, Lu S, Ouyang M, Lin L, Zhuo Y, Liu B, Chien S, Neel B, Wang Y. Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2. Nature Communications 2013, 4: 2037. PMID: 23792876, PMCID: PMC3777412, DOI: 10.1038/ncomms3037.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesEmbryo, MammalianExtracellular Signal-Regulated MAP KinasesFibroblastsFluorescence Resonance Energy TransferGenes, ReporterGRB2 Adaptor ProteinHEK293 CellsHumansKineticsMiceMolecular Sequence DataMutant ProteinsMutationPeptidesPhosphorylationPhosphotyrosineProtein BindingProtein ConformationProtein Tyrosine Phosphatase, Non-Receptor Type 11ConceptsCis-interactionsSH2 domainC-terminal phosphotyrosinesProtein tyrosine phosphatase SHP2Amino acid sequenceTyrosine phosphatase SHP2Adaptor proteinModular domainsModular proteinsTrans-regulationAcid sequenceProtein functionPhosphatase SHP2Evolutionary dynamicsBinding site affinityPhosphotyrosineConformational dynamicsProteinGrb2SH2SequenceSHP2Site affinityAntagonist combinationDominant form