1. A single gD glycoprotein can mediate infection by Herpes simplex virus.

    Journal of the American Chemical Society 135(30):11175 (2013) PMID 23837576 PMCID PMC3756529

    Herpes simplex viruses display hundreds of gD glycoproteins, and yet their neutralization requires tens of thousands of antibodies per virion, leading us to ask whether a wild-type virion with just a single free gD is still infective. By quantitative analysis of fluorescently labeled virus parti...
  2. A single gD glycoprotein can mediate infection by Herpes simplex virus.

    Journal of the American Chemical Society 135(30):11175 (2013) PMID 23837576 PMCID PMC3756529

    Herpes simplex viruses display hundreds of gD glycoproteins, and yet their neutralization requires tens of thousands of antibodies per virion, leading us to ask whether a wild-type virion with just a single free gD is still infective. By quantitative analysis of fluorescently labeled virus parti...
  3. Pipette-surface interaction: current enhancement and intrinsic force.

    Journal of the American Chemical Society 135(1):322 (2013) PMID 23210472

    There is an intrinsic repulsion between glass and cell surfaces that allows noninvasive scanning ion conductance microscopy (SICM) of cells and which must be overcome in order to form the gigaseals used for patch clamping investigations of ion channels. However, the interactions of surfaces in p...
  4. Pipette-surface interaction: current enhancement and intrinsic force.

    Journal of the American Chemical Society 135(1):322 (2013) PMID 23210472

    There is an intrinsic repulsion between glass and cell surfaces that allows noninvasive scanning ion conductance microscopy (SICM) of cells and which must be overcome in order to form the gigaseals used for patch clamping investigations of ion channels. However, the interactions of surfaces in p...
  5. Hydrodynamic trapping of molecules in lipid bilayers.

    PNAS 109(26):10328 (2012) PMID 22699491 PMCID PMC3387037

    In this work we show how hydrodynamic forces can be used to locally trap molecules in a supported lipid bilayer (SLB). The method uses the hydrodynamic drag forces arising from a flow through a conical pipette with a tip radius of 1-1.5 μm, placed approximately 1 μm above the investigated SLB. T...
  6. Hydrodynamic trapping of molecules in lipid bilayers.

    PNAS 109(26):10328 (2012) PMID 22699491 PMCID PMC3387037

    In this work we show how hydrodynamic forces can be used to locally trap molecules in a supported lipid bilayer (SLB). The method uses the hydrodynamic drag forces arising from a flow through a conical pipette with a tip radius of 1-1.5 μm, placed approximately 1 μm above the investigated SLB. T...
  7. Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

    Cell 149(5):1048 (2012)

    Here, we use single-molecule techniques to study the aggregation of α-synuclein, the protein whose misfolding and deposition is associated with Parkinson's disease. We identify a conformational change from the initially formed oligomers to stable, more compact proteinase-K-resistant ol...
  8. Direct observation of the interconversion of normal and toxic forms of α-synuclein.

    Cell 149(5):1048 (2012) PMID 22632969 PMCID PMC3383996

    Here, we use single-molecule techniques to study the aggregation of α-synuclein, the protein whose misfolding and deposition is associated with Parkinson's disease. We identify a conformational change from the initially formed oligomers to stable, more compact proteinase-K-resistant oligomers as...
  9. Direct observation of the interconversion of normal and toxic forms of α-synuclein.

    Cell 149(5):1048 (2012) PMID 22632969 PMCID PMC3383996

    Here, we use single-molecule techniques to study the aggregation of α-synuclein, the protein whose misfolding and deposition is associated with Parkinson's disease. We identify a conformational change from the initially formed oligomers to stable, more compact proteinase-K-resistant oligomers as...
  10. Direct observation of the interconversion of normal and toxic forms of α-synuclein.

    Cell 149(5):1048 (2012) PMID 22632969 PMCID PMC3383996

    Here, we use single-molecule techniques to study the aggregation of α-synuclein, the protein whose misfolding and deposition is associated with Parkinson's disease. We identify a conformational change from the initially formed oligomers to stable, more compact proteinase-K-resistant oligomers as...
  11. Direct observation of the interconversion of normal and toxic forms of α-synuclein.

    Cell 149(5):1048 (2012) PMID 22632969 PMCID PMC3383996

    Here, we use single-molecule techniques to study the aggregation of α-synuclein, the protein whose misfolding and deposition is associated with Parkinson's disease. We identify a conformational change from the initially formed oligomers to stable, more compact proteinase-K-resistant oligomers as...
  12. Investigating the Interaction Between Characterized Amyloid-Beta Oligomers and the Prion Protein Receptor in Live Cells

    Biophysical Journal 102(3):243a (2012)

  13. Single molecule fluorescence under conditions of fast flow.

    Analytical chemistry 84(1):179 (2012) PMID 22147688

    We have experimentally determined the optimal flow velocities to characterize or count single molecules by using a simple microfluidic device to perform two-color coincidence detection (TCCD) and single pair Förster resonance energy transfer (spFRET) using confocal fluorescence spectroscopy on m...
  14. Single molecule fluorescence under conditions of fast flow.

    Analytical chemistry 84(1):179 (2012) PMID 22147688

    We have experimentally determined the optimal flow velocities to characterize or count single molecules by using a simple microfluidic device to perform two-color coincidence detection (TCCD) and single pair Förster resonance energy transfer (spFRET) using confocal fluorescence spectroscopy on m...
  15. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.

    Nature Structural & Molecular Biology 19(1):79 (2012) PMID 22179788

    In recent genome-wide association studies, the extracellular chaperone protein, clusterin, has been identified as a newly-discovered risk factor in Alzheimer's disease. We have examined the interactions between human clusterin and the Alzheimer's disease-associated amyloid-β(1-40) peptide (Aβ(1-...
  16. The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide.

    Nature Structural & Molecular Biology 19(1):79 (2012) PMID 22179788

    In recent genome-wide association studies, the extracellular chaperone protein, clusterin, has been identified as a newly-discovered risk factor in Alzheimer's disease. We have examined the interactions between human clusterin and the Alzheimer's disease-associated amyloid-β(1-40) peptide (Aβ(1-...
  17. Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer.

    ChemPhysChem 12(3):491 (2011) PMID 20922742

    The use of Förster resonance energy transfer (FRET) as a tool to study biomolecules has been greatly enhanced by new advances in single-molecule fluorescence (SMF) techniques. This has allowed new insights into the structure and dynamics of complex biomolecular machinery. However, there are stil...
  18. Single-molecule fluorescence coincidence spectroscopy and its application to resonance energy transfer.

    ChemPhysChem 12(3):491 (2011) PMID 20922742

    The use of Förster resonance energy transfer (FRET) as a tool to study biomolecules has been greatly enhanced by new advances in single-molecule fluorescence (SMF) techniques. This has allowed new insights into the structure and dynamics of complex biomolecular machinery. However, there are stil...
  19. Fluorescence coincidence spectroscopy for single-molecule fluorescence resonance energy-transfer measurements.

    Analytical chemistry 80(22):8389 (2008) PMID 18855410

    Single-molecule fluorescence resonance energy transfer (FRET) is commonly used to probe different conformations and conformational dynamics of single biomolecules. However, the analysis of raw burst traces is not always straightforward. The presence of a "zero peak" and the skewness of peaks at ...
  20. Fluorescence coincidence spectroscopy for single-molecule fluorescence resonance energy-transfer measurements.

    Analytical chemistry 80(22):8389 (2008) PMID 18855410

    Single-molecule fluorescence resonance energy transfer (FRET) is commonly used to probe different conformations and conformational dynamics of single biomolecules. However, the analysis of raw burst traces is not always straightforward. The presence of a "zero peak" and the skewness of peaks at ...