Results 21 to 30 of about 5,805,397 (279)

Single-molecule FRET analysis software (v3.0)

, 2021
A Python package and several Jupyter notebooks to analyze single molecule FRET ...
Schrangl, Lukas
core   +1 more source

A versatile platform for single-molecule enzymology of restriction endonuclease [PDF]

Journal of Innovative Optical Health Sciences, 2019
Enzymes are the major players for many biological processes. Fundamental studies of the enzymatic activity at the single-molecule level provides important information that is otherwise inaccessible at the ensemble level.
Xin Wang, Jingyuan Nie, Yi Li, Hai Pan, Peng Zheng, Meng Qin, Yi Cao, Wei Wang   +7 more
doaj   +1 more source

FRET Based Biosensor: Principle Applications Recent Advances and Challenges

Diagnostics, 2023
Förster resonance energy transfer (FRET)-based biosensors are being fabricated for specific detection of biomolecules or changes in the microenvironment.
Awadhesh Kumar Verma, Ashab Noumani, Amit K. Yadav, Pratima R. Solanki   +3 more
doaj   +1 more source

Single-Molecule FRET Imaging of Virus Spike–Host Interactions

Viruses, 2021
As a major surface glycoprotein of enveloped viruses, the virus spike protein is a primary target for vaccines and anti-viral treatments. Current vaccines aiming at controlling the COVID-19 pandemic are mostly directed against the SARS-CoV-2 spike ...
Maolin Lu
doaj   +1 more source

Single-molecule chemical denaturation of riboswitches [PDF]

, 2013
To date, single-molecule RNA science has been developed almost exclusively around the effect of metal ions as folding promoters and stabilizers of the RNA structure.
St-Pierre, Patrick, Penedo, J Carlos, Dubé, Audrey, Samuel, Ifor D W, St-Pierre, P, Samuel, Ifor David William, Lafontaine, Daniel, Dalgarno, Paul Allan, Bordello, Jorge, Morris, Rhodri, Bordello, J, Penedo, Carlos, Lafontaine, Daniel A, Dubé, A., Dalgarno, Paul A; id_orcid, Samuel, Ifor David William; id_orcid, Penedo, Carlos; id_orcid   +16 more
core   +1 more source

Single-Molecule FRET Analyses of NMDA Receptors. [PDF]

Methods Mol Biol
Single-molecule fluorescence resonance energy transfer (smFRET) enables the real-time observation of conformational changes in a single protein molecule of interest. These observations are achieved by attaching fluorophores to proteins of interest in a site-specific manner and investigating the FRET between the fluorophores. Here we describe the method
Durham RJ, Jayaraman V.
europepmc   +3 more sources

Structural Changes of Yellow Cameleon Domains Observed by Quantitative FRET Analysis and Polarized Fluorescence Correlation Spectroscopy [PDF]

, 2008
Förster resonance energy transfer (FRET) is a widely used method for monitoring interactions between or within biological macromolecules conjugated with suitable donor-acceptor pairs.
Laptenok, S., Visser, N.V., Kalinin, S., Hornen, H., Hoek, A., van, Kühnemuth, R., Borst, J.W., van Hoek, A., Westphal, A.H., Aker, J., Aker, J.C.M., Kyhnemuth, R., Laptenok, S.P., Seidel, C.A.M., Visser, A.J.W.G.   +14 more
core   +1 more source

Build Your Own Microscope: Step-By-Step Guide for Building a Prism-Based TIRF Microscope

Methods and Protocols, 2018
Prism-based total internal reflection fluorescence (pTIRF) microscopy is one of the most widely used techniques for the single molecule analysis of a vast range of samples including biomolecules, nanostructures, and cells, to name a few.
Dalton R. Gibbs, Anisa Kaur, Anoja Megalathan, Kumar Sapkota, Soma Dhakal   +4 more
doaj   +1 more source

Protein folding studied by single-molecule FRET [PDF]

Current Opinion in Structural Biology, 2008
A complete understanding of a protein-folding mechanism requires description of the distribution of microscopic pathways that connect the folded and unfolded states. This distribution can, in principle, be described by computer simulations and theoretical models of protein folding, but is hidden in conventional experiments on large ensembles of ...
Schuler, B, Eaton, W A
openaire   +4 more sources

Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs [PDF]

, 2010
Förster resonance energy transfer (FRET) is a powerful method for obtaining information about small-scale lengths between biomacromolecules. Visible fluorescent proteins (VFPs) are widely used as spectrally different FRET pairs, where one VFP acts as a ...
Birch, D.J.S., Laptenok, S., Visser, N.V., Hoek, A., van, Laptenok, S.P., Borst, J.W., Visser, A.J.W.G., van Hoek, A., Brochon, J.C.   +8 more
core   +1 more source