News & Views in 2006

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.

Two new protein fragment complementation methods expand the toolkit available for the detection of protein interactions in living cells.

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.

A new twist to a classic technique offers a new way to accurately measure population diversity at the nucleic acid level.

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.

DNase-chip and DNase-array: similar names for two different new approaches that give a genomic perspective to the conventional DNase I hypersensitivity assay used to measure chromatin accessibility.

Two methods give genetics researchers new ways to uncover different forms of genomic structural variation. Based on a novel application of existing PCR technologies, they promise to make the study of DNA rearrangements accessible to a wider field.

A new method that barcodes cells by assigning different intensities of fluorescent dyes to differently treated samples allows the simultaneous processing of a large number of samples, as one pool, thus increasing the throughput of multidimensional cytometry.

A deceptively simple signal processing method allows researchers to quantify complex and irregular patterns of high frequency neuronal activity in whole brain at single-neuron resolution by deconvolving the slow Ca²⁺ signals generated by neuronal spikes.

The tight interaction between the small molecule biotin and the tetrameric protein streptavidin is widely exploited for many different applications in protein science. In this issue, researchers present the design of a monovalent streptavidin tetramer with a single biotin binding site and demonstrate its enhanced properties over wild-type streptavidin for use in cell-surface protein labeling.

A new approach to generating large quantities of myeloid progenitor cells ex vivo will facilitate detailed studies of normal white blood cell differentiation and of abnormalities leading to blood disorders such as leukemia.

A recently developed multigene viral expression system is put to work to generate mice carrying a single T-cell receptor (TCR) specificity. Complementing the transgenic-mice technique, this method offers new practical options to researchers studying T-cell development.

A simple 'smart-pooling' screening strategy for large-scale systems biology experiments promises to provide considerable improvement in experimental efficiency, while simultaneously allowing improved accuracy and coverage.

Intracellular protein-protein interactions form the basis of most biological processes. Structural aspects of these reactions can now be analyzed in living prokaryotic cells and in atomic detail by nuclear magnetic resonance spectroscopy.

Understanding of the sequelae of cerebral microvascular injury has been hampered by a lack of animal models to enable precise localization of injury. In this issue, Nishimura et al. describe a stroke model that couples two-photon laser-scanning mapping of the cerebral cortex with femtosecond laser technology to produce three distinct microvascular injuries characterized by hemorrhage, vessel leakage or vessel occlusion.