Results 11 to 20 of about 4,596 (191)
Developing Multichannel smFRET Approach to Dissecting Ribosomal Mechanisms
Chemical & Biomedical ImagingThe ribosome, a 2.6 megadalton biomolecule measuring approximately 20 nm in diameter, coordinates numerous ligands, factors, and regulators to translate proteins with high fidelity and speed. Understanding its complex functions necessitates multiperspective observations.
Yuhong Wang
exaly +5 more sources
Single-photon smFRET. I: Theory and conceptual basis
Biophysical Reports, 2023 We present a unified conceptual framework and the associated software package for single-molecule Förster resonance energy transfer (smFRET) analysis from single-photon arrivals leveraging Bayesian nonparametrics, BNP-FRET.
Ayush Saurabh +4 more
doaj +3 more sources
Single-photon smFRET: II. Application to continuous illumination
Biophysical Reports, 2023 Here we adapt the Bayesian nonparametrics (BNP) framework presented in the first companion article to analyze kinetics from single-photon, single-molecule Förster resonance energy transfer (smFRET) traces generated under continuous illumination.
Ayush Saurabh +4 more
doaj +3 more sources
Cotranslational Incorporation into Proteins of a Fluorophore Suitable for smFRET Studies
ACS Synthetic Biology, 2018 Single-molecule FRET (smFRET) is a powerful tool to investigate conformational changes of biological molecules. In general, smFRET studies require protein samples that are site-specifically double-labeled with a pair of donor and acceptor fluorophores.
Sadoine, Mayuri +4 more
openaire +4 more sources
An automated single-molecule FRET platform for high-content, multiwell plate screening of biomolecular conformations and dynamics [PDF]
Nature Communications, 2023 Single-molecule FRET (smFRET) has become a versatile tool for probing the structure and functional dynamics of biomolecular systems, and is extensively used to address questions ranging from biomolecular folding to drug discovery.
Andreas Hartmann +6 more
doaj +14 more sources
Parallel multispot smFRET analysis using an 8-pixel SPAD array [PDF]
SPIE Proceedings, 2012 Single-molecule Förster resonance energy transfer (smFRET) is a powerful tool for extracting distance information between two fluorophores (a donor and acceptor dye) on a nanometer scale. This method is commonly used to monitor binding interactions or intra- and intermolecular conformations in biomolecules freely diffusing through a focal volume or ...
INGARGIOLA, ANTONINO +9 more
openaire +4 more sources
Multiplexed smFRET Nucleic Acid Sensing Using DNA Nanotweezers
Biosensors, 2023 The multiplexed detection of disease biomarkers is part of an ongoing effort toward improving the quality of diagnostic testing, reducing the cost of analysis, and accelerating the treatment processes.
Anisa Kaur +4 more
doaj +3 more sources
Paving the way for structural modelling by smFRET measurements
, 2019 The thesis at hand contributes to the field of structure determination of bio-macromolecules. It focuses on the Förster resonance energy transfer (FRET), which allows to infer distances at the molecular level (≈ 2-10 nm) making FRET a promising tool for structure analysis.
Eilert, Tobias
openaire +3 more sources
Pathogenic mechanism of the K141E mutation in HSPB8: Insights from smFRET and simulations
Cell Stress and ChaperonesPathogenic mutations can have a large impact on the conformational ensemble of intrinsically disordered proteins, but revealing those effects and their physiological relevance can be challenging. We used large-scale all-atom explicit-solvent molecular dynamics simulations and single-molecule Förster resonance energy transfer (smFRET) experiments to ...
Daniele Montepietra +6 more
core +7 more sources
Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET [PDF]
Nature Communications, 2022 Pulsed electron-electron double resonance spectroscopy (PELDOR/DEER) and single-molecule Förster resonance energy transfer spectroscopy (smFRET) are used to determine conformational changes and probe distances in biological macromolecules.
Martin F. Peter +8 more
doaj +2 more sources