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Fluorescence resonance energy transfer at the single-molecule level
Fluorescence resonance energy transfer (FRET) is a powerful spectroscopic method for
measuring distances in the 2–8 nm range. Often, conformational changes and molecular …
measuring distances in the 2–8 nm range. Often, conformational changes and molecular …
Toward dynamic structural biology: Two decades of single-molecule Förster resonance energy transfer
BACKGROUND Biomolecular mechanisms are typically inferred from static structural
“snapshots” obtained by x-ray crystallography, nuclear magnetic resonance (NMR) …
“snapshots” obtained by x-ray crystallography, nuclear magnetic resonance (NMR) …
The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA
Abstract The SARS-CoV-2 nucleocapsid (N) protein is an abundant RNA-binding protein
critical for viral genome packaging, yet the molecular details that underlie this process are …
critical for viral genome packaging, yet the molecular details that underlie this process are …
Nanometer resolution imaging and tracking of fluorescent molecules with minimal photon fluxes
We introduce MINFLUX, a concept for localizing photon emitters in space. By probing the
emitter with a local intensity minimum of excitation light, MINFLUX minimizes the …
emitter with a local intensity minimum of excitation light, MINFLUX minimizes the …
Quantifying forster resonance energy transfer from single perovskite quantum dots to organic dyes
Colloidal quantum dots (QDs) are promising regenerable photoredox catalysts offering
broadly tunable redox potentials along with high absorption coefficients. QDs have thus far …
broadly tunable redox potentials along with high absorption coefficients. QDs have thus far …
Balanced protein–water interactions improve properties of disordered proteins and non-specific protein association
Some frequently encountered deficiencies in all-atom molecular simulations, such as
nonspecific protein–protein interactions being too strong, and unfolded or disordered states …
nonspecific protein–protein interactions being too strong, and unfolded or disordered states …
Protein ensembles: how does nature harness thermodynamic fluctuations for life? The diverse functional roles of conformational ensembles in the cell
All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …
Understanding protein adsorption phenomena at solid surfaces
M Rabe, D Verdes, S Seeger - Advances in colloid and interface science, 2011 - Elsevier
Protein adsorption at solid surfaces plays a key role in many natural processes and has
therefore promoted a widespread interest in many research areas. Despite considerable …
therefore promoted a widespread interest in many research areas. Despite considerable …
Wetting transition from the Cassie–Baxter state to the Wenzel state on textured polymer surfaces
The wetting transition from the Cassie–Baxter state to the Wenzel state on textured surfaces
was investigated. Nano-to microscale hexagonal pillared lattices were prepared by …
was investigated. Nano-to microscale hexagonal pillared lattices were prepared by …
Protein folding and misfolding
CM Dobson - Nature, 2003 - nature.com
The manner in which a newly synthesized chain of amino acids transforms itself into a
perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence …
perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence …