Search results for "Resonance energy transfer"

showing 10 items of 98 documents

Precision and accuracy of single-molecule FRET measurements-a multi-laboratory benchmark study

2018

Single-molecule Forster resonance energy transfer (smFRET) is increasingly being used to determine distances, structures, and dynamics of biomolecules in vitro and in vivo. However, generalized protocols and FRET standards to ensure the reproducibility and accuracy of measurements of FRET efficiencies are currently lacking. Here we report the results of a comparative blind study in which 20 labs determined the FRET efficiencies (E) of several dye-labeled DNA duplexes. Using a unified, straightforward method, we obtained FRET efficiencies with s.d. between +/- 0.02 and +/- 0.05. We suggest experimental and computational procedures for converting FRET efficiencies into accurate distances, and…

0301 basic medicinePHOTON DISTRIBUTIONDYNAMICSAccuracy and precisionTechnologyBiophysicsRESONANCE ENERGY-TRANSFERBiochemistryMedical and Health SciencesArticle03 medical and health sciencesBlind studySingle-molecule biophysicsALTERNATING-LASER EXCITATIONSTRUCTURAL INFORMATIONFluorescence resonance energy transferDEPENDENCEQuantitative assessmentLife ScienceFLUORESCENCEStructure determinationMolecular BiologyQCVLAGBiophysical methodsReproducibilityReproducibility of ResultsCell BiologySingle-molecule FRETDNABiological SciencesPublisher CorrectionQPSPECTROSCOPIC RULER030104 developmental biologyFörster resonance energy transferBiofysicaBenchmark (computing)Photon distributionEPSREFRACTIVE-INDEXLaboratoriesBiological systemBiotechnologyDevelopmental Biology
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Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”

2018

Editors at Science requested our input on the above discussion (comment by Best et al . and response by Riback et al .) because both sets of authors use our data from Fuertes et al . (2017) to support their arguments. The topic of discussion pertains to the discrepant inferences drawn from SAXS versus FRET measurements regarding the dimensions of intrinsically disordered proteins (IDPs) in aqueous solvents. Using SAXS measurements on labeled and unlabeled proteins, we ruled out the labels used for FRET measurements as the cause of discrepant inferences between the two methods. Instead, we propose that FRET and SAXS provide complementary readouts because of a decoupling of size and shape fl…

0301 basic medicinePhysicsMultidisciplinarySmall-angle X-ray scatteringScattering010402 general chemistryIntrinsically disordered proteins01 natural sciences0104 chemical sciences03 medical and health sciences030104 developmental biologyFörster resonance energy transferStatistical physicsDecoupling (electronics)Science
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Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers

2018

Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static "spring-loaded" fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, using single-molecule Förster resonance energy transfer (smFRET)-imaging, we directly visualized pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of p…

0301 basic medicineProtein ConformationHemagglutinin (influenza)Hemagglutinin Glycoproteins Influenza VirusBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyReaction coordinate03 medical and health sciencesViral envelopeInfluenza HumanFluorescence Resonance Energy TransferHumansDynamic equilibriumFusionCell MembraneLipid bilayer fusionHydrogen-Ion ConcentrationVirus InternalizationSingle Molecule ImagingHEK293 CellsHemagglutinins030104 developmental biologyMembraneFörster resonance energy transferA549 CellsInfluenza A virusBiophysicsbiology.proteinProtein BindingCell
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Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors

2016

Peripherin-2 is a glycomembrane protein exclusively expressed in the light-sensing compartments of rod and cone photoreceptors designated as outer segments (OS). Mutations in peripherin-2 are associated with degenerative retinal diseases either affecting rod or cone photoreceptors. While peripherin-2 has been extensively studied in rods, there is only little information on its supramolecular organization and function in cones. Recently, we have demonstrated that peripherin-2 interacts with the light detector rhodopsin in OS of rods. It remains unclear, however, if peripherin-2 also binds to cone opsins. Here, using a combination of co-immunoprecipitation analyses, transmission electron micr…

0301 basic medicineRhodopsinOpsingenetic structuresmacromolecular substances030105 genetics & heredityBiologymedicine.disease_causeRetinaMice03 medical and health scienceschemistry.chemical_compoundImmunolabelingMicroscopy Electron TransmissionAntigens NeoplasmFluorescence Resonance Energy TransferGeneticsmedicineAnimalsHumansPeripherin 2Molecular BiologyGenetics (clinical)MutationRetinal DegenerationRetinalGeneral MedicineCone Opsinseye diseases030104 developmental biologyFörster resonance energy transfernervous systemchemistryRhodopsinMutationRetinal Cone Photoreceptor CellsBiophysicsbiology.proteinsense organsProtein BindingVisual phototransductionHuman Molecular Genetics
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Associating HIV-1 envelope glycoprotein structures with states on the virus observed by smFRET

2019

The HIV-1 envelope glycoprotein (Env) trimer mediates cell entry and is conformationally dynamic1-8. Imaging by single-molecule fluorescence resonance energy transfer (smFRET) has revealed that, on the surface of intact virions, mature pre-fusion Env transitions from a pre-triggered conformation (state 1) through a default intermediate conformation (state 2) to a conformation in which it is bound to three CD4 receptor molecules (state 3)8-10. It is currently unclear how these states relate to known structures. Breakthroughs in the structural characterization of the HIV-1 Env trimer have previously been achieved by generating soluble and proteolytically cleaved trimers of gp140 Env that are …

0301 basic medicinechemistry.chemical_classificationMutationMultidisciplinary030102 biochemistry & molecular biologyStrain (chemistry)virusesHEK 293 cellsvirus diseasesTrimermedicine.disease_causeArticleVirus3. Good health03 medical and health sciences030104 developmental biologyFörster resonance energy transferProtein structurechemistryBiophysicsmedicineGlycoproteinNature
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Modulation of mitochondriotropic properties of cyanine dyes by in organello copper-free click reaction

2017

Cyanine (Cy) dyes show a general propensity to localize in polarized mitochondria. This mitochondriotropism was used to perform a copper-free click reaction in the mitochondria of living cells. The in organello reaction of dyes Cy3 and Cy5 led to a product that was easily traceable by Forster resonance energy transfer (FRET). As determined by confocal laser scanning microscopy, the Cy3-Cy5 conjugate showed enhanced retention in mitochondria, relative to that of the starting compounds. This enhancement of a favorable property can be achieved by synthesis in organello, but not outside mitochondria.

0301 basic medicinechemistry.chemical_elementBiochemistryCell Line03 medical and health scienceschemistry.chemical_compoundConfocal laser scanning microscopyFluorescence Resonance Energy TransferOrganic chemistryAnimalsCyanineMolecular BiologyFluorescent DyesMicroscopy ConfocalOrganic ChemistryfungiCarbocyaninesCopperMitochondriaRats030104 developmental biologyFörster resonance energy transferchemistryMitochondrial targetingClick chemistryBiophysicsMolecular MedicineClick ChemistryCopperConjugateChemBioChem
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FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices.

2021

International audience; Single-molecule FRET (smFRET) has become a mainstream technique for studying biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by an ever- increasing number of groups has generated significant progress in sample preparation, measurement procedures, data analysis, algorithms and documentation. Several labs that employ smFRET approaches have joined forces to inform the smFRET community about streamlining how to perform experiments and analyze results for obtaining quantitative information on biomolecular structure and dynamics. The recent efforts include blind tests to assess the accuracy and the precision of smFRET experiments among d…

0301 basic medicineconformationOpen scienceComputer scienceStructural Biology and Molecular BiophysicsAMINOACYL-TRANSFER-RNAINTRAMOLECULAR DISTANCE DISTRIBUTIONSReview ArticleRESONANCE ENERGY-TRANSFER01 natural sciencesbiomoleculesFREELY DIFFUSING MOLECULESDocumentationFluorescence Resonance Energy TransferMainstreamstructural biologyBiology (General)General NeuroscienceQRNANO-POSITIONING SYSTEMGeneral MedicinedynamicsINTRINSICALLY DISORDERED PROTEINSSingle Molecule ImagingFLUORESCENCE CORRELATION SPECTROSCOPY[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMedicinecommunitysingle-moleculeQH301-705.5ScienceAppeal[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsBioengineeringchemical biology010402 general chemistryGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesALTERNATING-LASER EXCITATIONBiochemistry and Chemical Biologymolecular biophysicsbiochemistryMolecular BiologyStructure (mathematical logic)General Immunology and MicrobiologySINGLE-MOLECULE FRETTRANSITION PATH TIMESData science0104 chemical sciences030104 developmental biologyFRETPosition paperGeneric health relevanceBiochemistry and Cell BiologyeLife
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Robust and sensitive GFP-based cGMP sensor for real time imaging in intact Caenorhabditis elegans

2018

AbstractcGMP is a ubiquitous second messenger that plays a role in sensory signaling and plasticity through its regulation of ion channels and kinases. Previous studies that primarily used genetic and biochemical tools suggest that cGMP is spatiotemporally regulated in multiple sensory modalities, including light, heat, gases, salt and odor. FRET- and GFP-based cGMP sensors were developed to visualize cGMP in primary cell culture and Caenorhabditis elegans to corroborate these findings. While a FRET-based sensor has been used in an intact animal to visualize cGMP, the requirement of a multiple emission system limits its ability to be used on its own as well as with other sensors and fluores…

0303 health sciencesbiologyChemistrybiology.organism_classificationCyclaseGreen fluorescent protein03 medical and health sciences0302 clinical medicinemedicine.anatomical_structureFörster resonance energy transferCell cultureSecond messenger systemmedicineBiophysicsNeuron030217 neurology & neurosurgeryCaenorhabditis elegansIon channel030304 developmental biology
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Agonist-induced formation of FGFR1 homodimers and signaling differ among members of the FGF family

2011

Fibroblast growth factor receptor 1 (FGFR1) is known to be activated by homodimerization in the presence of both the FGF agonist ligand and heparan sulfate glycosaminoglycan. FGFR1 homodimers in turn trigger a variety of downstream signaling cascades via autophosphorylation of tyrosine residues in the cytoplasmic domain of FGFR1. By means of Bioluminescence Energy Resonance Transfer (BRET) as a sign of FGFR1 homodimerization, we evaluated in HEK293T cells the effects of all known FGF agonist ligands on homodimer formation. A significant correlation between BRET(2) signaling and ERK1/2 phosphorylation was observed, leading to a further characterization of the binding and signaling properties…

AgonistMAPK/ERK pathwaymedicine.drug_classBiophysicsSettore BIO/11 - Biologia MolecolareBiologyLigandsFibroblast growth factorSettore BIO/09 - FisiologiaBiochemistrychemistry.chemical_compoundFluorescence Resonance Energy TransfermedicineHumansReceptor Fibroblast Growth Factor Type 1Molecular BiologyMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Fibroblast growth factor receptor 1HEK 293 cellsAutophosphorylationCell BiologyHeparan sulfateFibroblast growth factors FGFR1 Homodimerization BRET MAPKCell biologyFibroblast Growth Factorsstomatognathic diseasesHEK293 CellschemistrySettore BIO/14 - FarmacologiaPhosphorylationHeparitin SulfateProtein MultimerizationBiochemical and Biophysical Research Communications
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Fibroblast Growth Factor Receptor 1– 5-Hydroxytryptamine 1A Heteroreceptor Complexes and Their Enhancement of Hippocampal Plasticity

2011

Background The hippocampus and its 5-hydroxytryptamine transmission plays an important role in depression related to its involvement in limbic circuit plasticity. Methods The analysis was made with bioluminescence resonance energy transfer, co-immunoprecipitation, in situ proximity ligation assay, binding assay, in cell western and the forced swim test. Results Using bioluminescence resonance energy transfer analysis, fibroblast growth factor receptor 1 (FGFR1)-5-hydroxytryptamine 1A (5-HT1A) receptor complexes have been demonstrated and their specificity and agonist modulation characterized. Their presence based on co-immunoprecipitation and proximity ligation assay has also been indicated…

Agonistmedicine.medical_specialtyReceptor complexmedicine.drug_classProximity ligation assayBiologyHippocampal formationTransfectionHeteroreceptorSettore BIO/09 - FisiologiaHippocampusRats Sprague-DawleyGrowth factor receptorInternal medicineFluorescence Resonance Energy TransfermedicineAnimalsHumansImmunoprecipitationReceptor Fibroblast Growth Factor Type 1Enzyme InhibitorsRNA Small InterferingCells CulturedBiological PsychiatryNeurons8-Hydroxy-2-(di-n-propylamino)tetralinNeuronal PlasticityDose-Response Relationship DrugFibroblast growth factor receptor 1Computational BiologyAllosteric modulation depression fibroblast growth factor receptor heteroreceptor neuronal plasticity serotonin receptorsRatsSerotonin Receptor AgonistsCell biologyEndocrinologyAnimals NewbornFibroblast growth factor receptorReceptor Serotonin 5-HT1AFibroblast Growth Factor 2PeptidesSignal TransductionBiological Psychiatry
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