about
Ultrastable atomic force microscopy: atomic-scale stability and registration in ambient conditionsOptimizing 1-μs-Resolution Single-Molecule Force Spectroscopy on a Commercial Atomic Force Microscope.Atomic force microscopy with sub-picoNewton force stability for biological applications.Stabilization of an optical microscope to 0.1 nm in three dimensions.Precision surface-coupled optical-trapping assay with one-basepair resolution.Integrating a high-force optical trap with gold nanoposts and a robust gold-DNA bond.Back-scattered detection provides atomic-scale localization precision, stability, and registration in 3D.Label-free optical imaging of membrane patches for atomic force microscopy.Single-molecule optical-trapping measurements with DNA anchored to an array of gold nanoposts.Optimizing bead size reduces errors in force measurements in optical traps.Ultrastable atomic force microscopy: improved force and positional stability.Ultrastable measurement platform: sub-nm drift over hours in 3D at room temperature.Optimizing force spectroscopy by modifying commercial cantilevers: Improved stability, precision, and temporal resolution.Routine and timely sub-picoNewton force stability and precision for biological applications of atomic force microscopy.Sequence-dependent nanometer-scale conformational dynamics of individual RecBCD-DNA complexesÅngström-precision optical traps and applications.Sequence-dependent pausing of single lambda exonuclease molecules.Rapid Characterization of a Mechanically Labile α-Helical Protein Enabled by Efficient Site-Specific Bioconjugation.Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.Improved Force Spectroscopy Using Focused-Ion-Beam-Modified Cantilevers.Single-molecule studies of RecBCD.Nano-chemical infrared imaging of membrane proteins in lipid bilayers.A Surface-Coupled Optical Trap with 1-bp Precision via Active Stabilization.Going Vertical To Improve the Accuracy of Atomic Force Microscopy Based Single-Molecule Force Spectroscopy.Force-activated DNA substrates for probing individual proteins interacting with single-stranded DNA.Improved Free-Energy Landscape Quantification Illustrated with a Computationally Designed Protein-Ligand Interaction.Force Spectroscopy with 9-μs Resolution and Sub-pN Stability by Tailoring AFM Cantilever Geometry.Direct Observation of the Reversible Two-State Unfolding and Refolding of an α/β Protein by Single-Molecule Atomic Force Microscopy.Relaxation of a single DNA molecule observed by optical microscopy.Improved free-energy landscape reconstruction of bacteriorhodopsin highlights local variations in unfolding energy.FEATHER: Automated Analysis of Force Spectroscopy Unbinding and Unfolding Data via a Bayesian AlgorithmHigh-Precision Single-Molecule Characterization of the Folding of an HIV RNA Hairpin by Atomic Force MicroscopyTFIIA Changes the Conformation of the DNA in TBP/TATA Complexes and Increases their Kinetic StabilityStretching of a single tethered polymer in a uniform flowSingle polymer dynamics in an elongational flowSelf-diffusion of an entangled DNA molecule by reptationDynamics and multiple stable binding modes of DNA intercalators revealed by single-molecule force spectroscopyOverstretching DNA at 65 pN does not require peeling from free ends or nicksImproved single molecule force spectroscopy using micromachined cantileversBending and looping of long DNA by Polycomb repressive complex 2 revealed by AFM imaging in liquid
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description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Thomas T Perkins
@ast
Thomas T Perkins
@en
Thomas T Perkins
@es
Thomas T Perkins
@nl
Thomas T Perkins
@sl
type
label
Thomas T Perkins
@ast
Thomas T Perkins
@en
Thomas T Perkins
@es
Thomas T Perkins
@nl
Thomas T Perkins
@sl
prefLabel
Thomas T Perkins
@ast
Thomas T Perkins
@en
Thomas T Perkins
@es
Thomas T Perkins
@nl
Thomas T Perkins
@sl
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P108
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0000-0003-4826-9490