Interaction dynamics of intrinsically disordered proteins from single-molecule spectroscopy
Many proteins contain large structurally disordered regions or are entirely disordered under
physiological conditions. The functions of these intrinsically disordered proteins (IDPs) often …
physiological conditions. The functions of these intrinsically disordered proteins (IDPs) often …
FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices
Single-molecule FRET (smFRET) has become a mainstream technique for studying
biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by …
biomolecular structural dynamics. The rapid and wide adoption of smFRET experiments by …
Single-molecule FRET for probing nanoscale biomolecular dynamics
Single-molecule spectroscopy is a powerful method for studying the physics of molecular
systems, particularly biomolecules, such as proteins and nucleic acids. By avoiding …
systems, particularly biomolecules, such as proteins and nucleic acids. By avoiding …
Resolving distance variations by single-molecule FRET and EPR spectroscopy using rotamer libraries
Förster resonance energy transfer (FRET) and electron paramagnetic resonance (EPR)
spectroscopy are complementary techniques for quantifying distances in the nanometer …
spectroscopy are complementary techniques for quantifying distances in the nanometer …
Accurate transfer efficiencies, distance distributions, and ensembles of unfolded and intrinsically disordered proteins from single-molecule FRET
Intrinsically disordered proteins (IDPs) sample structurally diverse ensembles.
Characterizing the underlying distributions of conformations is a key step toward …
Characterizing the underlying distributions of conformations is a key step toward …
Single-molecule counting applied to the study of GPCR oligomerization
Single-molecule counting techniques enable a precise determination of the intracellular
abundance and stoichiometry of proteins and macromolecular complexes. These details are …
abundance and stoichiometry of proteins and macromolecular complexes. These details are …
Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction
M Guillien, A Mouhand, A Sagar, A Fournet… - Structure, 2023 - cell.com
Arrestin-dependent G protein-coupled receptor (GPCR) signaling pathway is regulated by
the phosphorylation state of GPCR's C-terminal domain, but the molecular bases of arrestin …
the phosphorylation state of GPCR's C-terminal domain, but the molecular bases of arrestin …
Single-molecule-binding studies of antivirals targeting the hepatitis C virus core protein
S Nepal, ED Holmstrom - Journal of Virology, 2023 - Am Soc Microbiol
The hepatitis C virus (HCV) core protein (HCVcp) is the most highly conserved protein
encoded by the HCV genome, and its N-terminal domain (NTDHCVcp) plays a crucial role in …
encoded by the HCV genome, and its N-terminal domain (NTDHCVcp) plays a crucial role in …
Integrating single-molecule FRET and biomolecular simulations to study diverse interactions between nucleic acids and proteins
JC Sanders, ED Holmstrom - Essays in biochemistry, 2021 - portlandpress.com
The conformations of biological macromolecules are intimately related to their cellular
functions. Conveniently, the well-characterized dipole–dipole distance-dependence of …
functions. Conveniently, the well-characterized dipole–dipole distance-dependence of …
Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET
N Bustorff, J Fitter - Biomolecules, 2023 - mdpi.com
A protein fold is defined as a structural arrangement of a secondary structure in a three-
dimensional space. It would be interesting to know whether a particular fold can be assigned …
dimensional space. It would be interesting to know whether a particular fold can be assigned …