Results 81 to 90 of about 6,254 (216)

Efficient use of single molecule time traces to resolve kinetic rates, models and uncertainties

open access: yes, 2017
Single molecule time traces reveal the time evolution of unsynchronized kinetic systems. Especially single molecule F\"orster resonance energy transfer (smFRET) provides access to enzymatically important timescales, combined with molecular distance ...
Hugel, Thorsten, Schmid, Sonja
core   +1 more source

A competition smFRET assay to study ligand‐induced conformational changes of the dengue virus protease

open access: yesProtein Science, 2022
Ligand binding to proteins often is accompanied by conformational transitions. Here, we describe a competition assay based on single molecule Förster resonance energy transfer (smFRET) to investigate the ligand‐induced conformational changes of the ...
Hannah Maus   +4 more
semanticscholar   +1 more source

Differences in Src phosphorylation of PSD‐93 and PSD‐95 drive differences in scaffolding activity

open access: yesProtein Science, Volume 35, Issue 2, February 2026.
Abstract Scaffold proteins contain multiple binding modules that allow for co‐localization of proteins that lack a direct interaction. Evolution resulted in different combinations of binding modules that rewired existing signal transduction pathways.
Frank A. Mindlin   +3 more
wiley   +1 more source

Single-molecule FRET reveals proofreading complexes in the large fragment of Bacillus stearothermophilus DNA polymerase I

open access: yesAIMS Biophysics, 2018
There is increasing interest in the use of DNA polymerases (DNA pols) in next-generation sequencing strategies. These methodologies typically rely on members of the A and B family of DNA polymerases that are classified as high-fidelity DNA polymerases ...
Thomas V. Christian   +1 more
doaj   +1 more source

Activated GTPase movement on an RNA scaffold drives co-translational protein targeting [PDF]

open access: yes, 2012
Approximately one-third of the proteome is initially destined for the eukaryotic endoplasmic reticulum or the bacterial plasma membrane. The proper localization of these proteins is mediated by a universally conserved protein-targeting machinery, the ...
Akopian, David   +4 more
core   +1 more source

IDPEnsembleTools: An open‐source library for analysis of conformational ensembles of disordered proteins

open access: yesProtein Science, Volume 35, Issue 1, January 2026.
Abstract Intrinsically disordered proteins (IDPs) lack stable tertiary structure and instead exist as dynamic ensembles of conformations, playing essential roles in cellular regulation, signaling, and disease. As structural ensembles of IDPs become increasingly available through databases such as the Protein Ensemble Database (PED) and various ...
Hamidreza Ghafouri   +3 more
wiley   +1 more source

Calibrated Langevin dynamics simulations of intrinsically disordered proteins

open access: yes, 2014
We perform extensive coarse-grained (CG) Langevin dynamics simulations of intrinsically disordered proteins (IDPs), which possess fluctuating conformational statistics between that for excluded volume random walks and collapsed globules.
Ho, Po-Yi   +2 more
core   +1 more source

Experiment-friendly kinetic analysis of single molecule data in and out of equilibrium

open access: yes, 2016
We present a simple and robust technique to extract kinetic rate models and thermodynamic quantities from single molecule time traces. SMACKS (Single Molecule Analysis of Complex Kinetic Sequences) is a maximum likelihood approach that works equally well
Götz, Markus   +2 more
core   +1 more source

smFRET reveals DHX36 repetitive binding,not unfolding,of G-quadruplexes

open access: yes, 2021
Our data challenge Chen et al.'s interpretation of smFRET results, i.e. the repetitive unfolding of G4 with one-base translocations. We believe that the observed oscillatory curve represents the alternate binding of DHX36 to the 3' and 5'G-tetrad of G4s, rather than the repetitive unfolding between the canonical and the transformed non-canonical G4s ...
Guo, Hai-Lei, Liu, Na-Nv, Xi, Xu-Guang
openaire   +2 more sources

smFRET Probing Reveals Substrate-Dependent Conformational Dynamics of E. coli Multidrug MdfA [PDF]

open access: yesBiophysical Journal, 2019
Bacterial multidrug-resistance transporters of the major facilitator superfamily are distinguished by their extraordinary ability to bind structurally diverse substrates, thus serving as a highly efficient tool to protect cells from multiple toxic substances present in their environment, including antibiotic drugs.
Yongping, Zhu   +4 more
openaire   +2 more sources

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