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Stable-isotope labelling by amino acids in cell culture (SILAC) has emerged as a simple and powerful format for quantitative proteomics. What are the current applications for SILAC? And, how will this technology be used in the future?
Several new optical microscopy techniques have recently emerged that each use different combinations of photon properties. These combinatorial microscopy techniques allow the visualization of location, orientation, motion and environment of proteins and organelles well below the classic resolution limit.
Recently, a method was developed to encode unnatural amino acids genetically in bacteria, yeast and mammalian cells. This provides a powerful tool for exploring protein structure and functionin vitro and in vivo, and for generating proteins with new or enhanced properties.
Fluorescence microscopy is a powerful tool to assay biological processes in intact living cells. Now, fluorescence microscopy is becoming a quantitative and high-throughput technology that can be applied to functional genomics experiments and can provide data for systems-biology approaches.
Protein-chip technology is a powerful tool for high-throughput assays of protein profiling, protein–DNA interactions and enzyme activity. Improvements in the technology, such as the construction of whole-proteome arrays in yeast, could lead to the description of comprehensive interaction maps in many organisms.
The visualization of protein complexes in living cells enables the investigation of molecular interactions in their native environment. Bimolecular fluorescence complementation analysis has been used to visualize protein interactions and modifications in different cell types and species.
Cryo-electron tomography is an emerging imaging technique that will allow us to map molecular landscapes inside cells. This 'visual proteomics' will complement and extend mass-spectrometry-based inventories, and will provide a quantitative description of the macromolecular interactions that underlie cellular functions.
