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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.
Getting cultured cells to 'do their job'—either to recreate in vivo function in an artificial setting or to churn out immense volumes of protein on command—requires both an understanding of the demands of cell physiology and the technology to meet those demands. Michael Eisenstein looks at contemporary solutions for culture conundrums.