Results 1 to 10 of about 3,262 (111)
Biophysica, 2022 Single-molecule Förster resonance energy transfer (smFRET) enables the deconvolution of various conformational substates of biomolecules. Over the past two decades, it has been widely used to understand the conformational dynamics of enzymes.
Bhaswati Sengupta
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Benchmarking dynamic analysis methods in diffusion-based single-molecule FRET [PDF]
Cell Reports: MethodsSummary: Single-molecule Förster resonance energy transfer (smFRET) provides nanometer-scale snapshots of biomolecular conformational dynamics, but extracting reliable dynamic information from diffusion-based measurements requires a careful choice of ...
Joel A. Crossley
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Contribution of smFRET to Chromatin Research
Biophysica, 2023 Chromatins are structural components of chromosomes and consist of DNA and histone proteins. The structure, dynamics, and function of chromatins are important in regulating genetic processes. Several different experimental and theoretical tools have been
Bhaswati Sengupta
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A Standardized Prism-Based TIRF Platform for Quantitative Single-Molecule Fluorescence Studies of Biomolecular Dynamics [PDF]
BiosensorsSingle-molecule Förster resonance energy transfer (smFRET) enables direct measurement of nanoscale conformational dynamics and heterogeneity in biomolecules, but quantitative interpretation of smFRET data critically depends on well-controlled excitation ...
Arijit Patra +4 more
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A Universal Protein Ladder for Standardization of Diverse FRET Assays [PDF]
Advanced ScienceFluorescence resonance energy transfer (FRET) is the highly distance dependent (3–10 nm) transfer of energy from a donor to an acceptor fluorophore, with transfer efficiency inversely proportional to the distance between the fluorophores.
Evelyn R. Smith +5 more
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In-cell single-molecule FRET measurement of cytosolic RAF proteins to investigate the structural states and kinetics among them [PDF]
Frontiers in Molecular BiosciencesThe structure of a protein is closely linked to its function. Many proteins undergo conformational changes while working in living cells. Consequently, proteins in various structural states coexist in the native cellular environment.
Kenji Okamoto, Yasushi Sako
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ABEL-FRET bridges the timescale gap in single-molecule measurements of the structural dynamics in the A2A adenosine receptor [PDF]
Communications ChemistryThe functional complexity of G protein-coupled receptors (GPCRs) arises from their structural dynamics, spanning timescales from nanoseconds to minutes.
Ivan Maslov +7 more
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Micromachines, 2021 Single-molecule Förster resonance energy transfer (smFRET) inherits the strategy of measurement from the effective “spectroscopic ruler” FRET and can be utilized to observe molecular behaviors with relatively high throughput at nanometer scale.
Yi Qiao +4 more
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eLife, 2021 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 ...
Eitan Lerner +45 more
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Single-Molecule FRET: A Tool to Characterize DNA Nanostructures
Frontiers in Molecular Biosciences, 2022 DNA nanostructures often involve temporally evolving spatial features. Tracking these temporal behaviors in real time requires sophisticated experimental methods with sufficiently high spatial and temporal resolution.
Nibedita Pal
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