Results 51 to 60 of about 6,254 (216)
Single-molecule microscopy reveals new insights into nucleotide selection by DNA polymerase I. [PDF]
, 2012 The mechanism by which DNA polymerases achieve their extraordinary accuracy has been intensely studied because of the linkage between this process and mutagenesis and carcinogenesis. Here, we have used single-molecule fluorescence microscopy to study the
Markiewicz, RP +3 more
core +1 more source
smFRET Detection of Cis and Trans DNA Interactions by the BfiI Restriction Endonuclease
Journal of Physical Chemistry B, 2023 Protein–DNA interactions are fundamental to many biological processes. Proteins must find their target site on a DNA molecule to perform their function, and mechanisms for target search differ across proteins.
Š. Ivanovaitė +9 more
semanticscholar +1 more source
Multiperspective smFRET reveals rate-determining late intermediates of ribosomal translocation [PDF]
Nature Structural & Molecular Biology, 2016 Directional translocation of the ribosome through the mRNA open reading frame is a critical determinant of translational fidelity. This process entails a complex interplay of large-scale conformational changes within the actively translating particle, which together coordinate the movement of tRNA and mRNA substrates with respect to the large and small
Wasserman, Michael R. +3 more
openaire +2 more sources
FRETBursts: An Open Source Toolkit for Analysis of Freely-Diffusing Single-Molecule FRET.
PLoS ONE, 2016 Single-molecule Förster Resonance Energy Transfer (smFRET) allows probing intermolecular interactions and conformational changes in biomacromolecules, and represents an invaluable tool for studying cellular processes at the molecular scale.
Antonino Ingargiola +4 more
doaj +1 more source
Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET
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 +1 more source
Journal of Physical Chemistry B, 2023 The structural flexibility of proteins is crucial for their functions. Many experimental and computational approaches can probe protein dynamics across a range of time and length-scales.
A. KrishnaMohan +4 more
semanticscholar +1 more source
Nature Communications, 2022 Slippery sequences in mRNA can cause the ribosome to change its reading frame. Using smFRET, Poulis et al. show how reversible fluctuations of peptidyl-tRNA slow down translocation, alter ribosome dynamics, and favor spontaneous ribosome frameshifting.
Panagiotis Poulis +3 more
doaj +1 more source
Conformational dynamics of a single protein monitored for 24 hours at video rate [PDF]
, 2018 We use plasmon rulers to follow the conformational dynamics of a single protein for up to 24 h at a video rate. The plasmon ruler consists of two gold nanospheres connected by a single protein linker.
Ahijado-Guzmán, Rubén +10 more
core +3 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 +3 more sources
Bio-Protocol, 2018 Single-molecule FRET (smFRET) is a powerful tool to investigate molecular structures and conformational changes of biological molecules. The technique requires protein samples that are site-specifically equipped with a pair of donor and acceptor ...
Mayuri Sadoine +3 more
doaj +1 more source