Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Artist's rendition of protein-protein interactions, using images provided by Marc Brehme and Giulio Superti-Furga, Ulf Landegren, Moritz Rossner and Simon Scheuring. Cover by Erin Boyle. Articles p1013, p995, p985 and p1007
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 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.
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.
