Results 31 to 40 of about 4,500 (194)
Conformational Selection and Induced Fit: The Behavior of Two Homologous Proteases
ChemistryEurope, 2023 Protein‐ligand interactions are crucial for many cellular processes, with details of the binding mechanism being discussed as essential for biological functions.
Hannah Maus +4 more
doaj +1 more source
A Continuous Time Representation of smFRET for the Extraction of Rapid Kinetics [PDF]
Biophysical Journal, 2020 Abstract Our goal is to learn kinetic rates from single molecule FRET (smFRET) data even if these exceed the data acquisition rate. To achieve this, we develop a variant of our recently proposed hidden Markov jump process (HMJP) with which we learn transition kinetics from parallel ...
Zeliha Kilic +5 more
openaire +2 more sources
Exploring Intra- and Inter-Regional Interactions in the IDP α-Synuclein Using smFRET and MD Simulations [PDF]
, 2023 Theoretical concepts from polymer physics are often used to describe intrinsically disordered proteins (IDPs). However, amino acid interactions within and between regions of the protein can lead to deviations from typical polymer scaling behavior and ...
Driver, Mark D. +8 more
core +3 more sources
PLoS Computational Biology, 2020 Molecular Dynamics (MD) simulations seek to provide atomic-level insights into conformationally dynamic biological systems at experimentally relevant time resolutions, such as those afforded by single-molecule fluorescence measurements.
Dylan Girodat +4 more
doaj +1 more source
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
The Polymers of Life: Exploring Cellular Function Through Polymer Concepts. [PDF]
Adv Sci (Weinh)Biomolecular phase separation reveals that a hidden layer of cellular organization is governed by the principles of polymer science. This review bridges polymer physics and cell biology, offering a primer on fundamental concepts, proposing a framework for interrogating cellular function, and synthesizing biophysical methods for decoding macromolecular ...
Chen M, Chilkoti A.
europepmc +2 more sources
Angewandte Chemie, EarlyView.Modifying the conformational ensemble of “molten‐globule” protein by the site‐specific incorporation of stereoisomeric 4‐fluoroproline residues modulated its binding affinity and aggregation behavior. 19F NMR spectroscopy enabled the detection of key interactions responsible for structural and dynamic changes. ABSTRACT Recently, the application of deep
Abir Ben Bouzayene +5 more
wiley +2 more sources
Nature Communications, 2023 Growing RNAs fold differently as they are transcribed, which modulates their finally adopted structures. Riboswitches regulate gene expression by structural change, which are sensitive to co-transcriptionally structural biology.
Yanyan Xue +5 more
doaj +1 more source
Time-resolved burst variance analysis
Biophysical Reports, 2023 Quantifying biomolecular dynamics has become a major task of single-molecule fluorescence spectroscopy methods. In single-molecule Förster resonance energy transfer (smFRET), kinetic information is extracted from the stream of photons emitted by attached
Ivan Terterov +3 more
doaj +1 more source