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A new method for analyzing membrane protein oligomerization by bioluminescence resonance energy transfer (BRET) suggests that dimerization of G protein–coupled receptors (GPCRs) may not be as prevalent as commonly believed.
Protein-protein interactions are at the heart of the cellular machinery. Direct in-cell visualization of single, endogenous protein interaction pairs now becomes possible.
A novel atomic force microscopy (AFM) setup allows researchers to image and manipulate unsupported membrane proteins separating two aqueous compartments. This promises to permit new detailed measurements of protein conformational changes and interactions under native-like conditions.
Affinity purification combined with mass spectrometry (AP-MS) is an increasingly important tool for both high-throughput and low-throughput analysis of stable protein complexes in cells. Two groups further expand the capabilities of this experimental approach.
Methods to simultaneously localize the positions of multiple single fluorophores by precisely determining their individual positions are now yielding impressive gains in fluorescence microscopy resolution.
The combination of appropriate labeling and a new imaging software allows researchers to follow the progress of individual HIV particles within infected cells with outstanding precision.
DNA containing a new unnatural base pair may be amplified by PCR and transcribed into RNA, potentially increasing the diversity available from nucleic acids.
In this issue, the Withers laboratory takes advantage of the negatively charged sialic acid to develop a high-throughput screening technology that can be used for evolving glycosyltransferases with new enzymatic activities.