Commentary in 2007

Next-generation sequencing technologies are beginning to facilitate genome sequencing. But in addition, new applications and new assay concepts have emerged that are vastly increasing our ability to understand genome function.

A new generation of non-Sanger-based sequencing technologies has delivered on its promise of sequencing DNA at unprecedented speed, thereby enabling impressive scientific achievements and novel biological applications. However, before stepping into the limelight, next-generation sequencing had to overcome the inertia of a field that relied on Sanger-sequencing for 30 years.

When generating novel tailor-made proteins, protein engineers routinely apply the principles of 'Darwinian' evolution. However, laboratory evolution of proteins also has the potential to test evolutionary theories and reproduce evolutionary scenarios, thus reconstructing putative protein intermediates and providing a glimpse of 'protein fossils'. This commentary describes research at the interface of applied and fundamental molecular evolution, and provides a personal view of how synergy between fundamental and applied experiments indicates novel and more efficient ways of generating new proteins in the laboratory.

To characterize the contributions of individual amino acids to the structure or function of a protein, researchers have adopted directed evolution approaches, which use iterated cycles of mutagenesis and selection or screening to search vast areas of sequence space for sets of mutations that provide insights into the protein of interest.

Research performed where epidemics hit the hardest is necessary to bring solutions to the major health crises that plague poverty-stricken areas. Far from being limited to these areas, 'research in situ' can benefit health management worldwide. There are pressing technological needs to be addressed in order to facilitate such research.

Mass spectrometry has been rapidly maturing as the core technology at the heart of proteomics. The application of these powerful methods to the study of human diseases and their translation to the clinic, however, has been beset with unique challenges.

ProteomeBinders is a new European consortium aiming to establish a comprehensive resource of well-characterized affinity reagents, including but not limited to antibodies, for analysis of the human proteome. Given the huge diversity of the proteome, the scale of the project is potentially immense but nevertheless feasible in the context of a pan-European or even worldwide coordination. NOTE: In the version of the article originally published, Manfred Koegl’s name was misspelled. Additionally, Zoltan Konthur's affiliation was listed incorrectly; it should be Max Planck Institute for Molecular Genetics, 14195 Berlin, Germany. These errors have been corrected in the HTML and PDF versions of the article.