Here we introduce the fully quantified spectral imaging (FSI) method as a new tool to probe
the stoichiometry and stability of protein complexes in biological membranes. The FSI …

Förster resonance energy transfer (FRET) between fluorophores of the same species was
recognized in the early to mid-1900s, well before modern heterotransfer applications …

FRET is an indispensable experimental tool for studying membrane proteins. Currently, two
models are available for researchers to determine the oligomerization state of membrane …

Förster resonance energy transfer (FRET) is a widely used technique for nanoscale
molecular distance measurements, which makes FRET ideal for studying protein …

Förster resonance energy transfer (FRET) spectrometry is a method for determining the
quaternary structure of protein oligomers from distributions of FRET efficiencies that are …

Understanding the photophysical properties of fluorescent proteins (FPs), such as emission
and absorption spectra, molecular brightness, photostability, and photo-switching, is critical …

Transmembrane proteins known as G protein-coupled receptors (GPCRs) have been shown
to form functional homo-or hetero-oligomeric complexes, although agreement has been …

While the notion that G protein-coupled receptors (GPCRs) associate into homo-and hetero-
oligomers has gained more recognition in recent years, a lack of consensus remains among …

Fluorescence emission is common in plants. While fluorescence microscopy has been
widely used to study living plants, its application in quantifying the fluorescence of fossil …

G-protein-coupled receptors (GPCRs) control vital cellular signaling pathways. GPCR
oligomerization is proposed to increase signaling diversity. However, many reports have …