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Structure, function, interaction

Posted: 23 May 2006 | | No comments yet

In the last decade proteomics has revolutionised biology and now biology starts revolutionising proteomics.

In the last decade proteomics has revolutionised biology and now biology starts revolutionising proteomics.

In the last decade proteomics has revolutionised biology and now biology starts revolutionising proteomics.

We are at an exciting interface where the biological questions we can ask and answer with proteomics have become less limited by the available technology and push proteomics towards new frontiers. Exploring these frontiers is the topic of the upcoming joint BSPR/EBI conference entitled ‘Integrative Proteomics: Structure, Function, Interaction’. The conference focuses on the new challenges in proteomics, which are about functions, mechanisms and global contexts rather than cataloguing components. The programme addresses key developments and applications featuring topical sessions with eminent speakers and short talks chosen from submitted abstracts. The full programme is available from http://www.bspr.org

Protein identification by mass spectrometry (MS) has become routine. Importantly, deciphering the components does not automatically reveal how they work together, just like dissecting the components of a house would leave a pile of bricks rather than a fair account of the architecture. Decisive advances are coming from multi-pronged approaches that will be discussed in the first five sessions. Quantitative proteomics (Session I) is one breakthrough that appears in many variations and has spawned a wide array of extremely useful applications. Quantitative data improve the fidelity and information content of proteomics experiments, and open the door to functional analysis on a systems biology level. Further advances in MS (Session IV), especially regarding resolution, mass accuracy, sensitivity and novel fragmentation methods, give us more comprehensive and accurate information about proteins. The session also will discuss new applications such as using MS as a molecular mass microscope to examine tissues. Of course, none of these exploits would be possible without continuous improvements in bioinformatics (Session V). Generating common standards for proteomic experiments may seem a boring exercise, but this is ‘mortar that makes bricks’ architecture. Without standards we are unable to compare proteomic information and integrate it with genomic and metabolomic data to obtain a holistic view of the state of an organism. This, the holy grail of biomedical research, already scintillates in front of our eyes when looking at simple microorganisms, where we can achieve the marriage between descriptive and functional data (Session III). At the other end of the spectrum we have our very incomplete, but increasingly successful attempts to utilise proteomics for the description and diagnosis of human diseases (Session II). Another key to understand function is the mapping of post-translational modifications (PTM) that govern the activity of enzymes (Session VI). MS is a powerful looking-glass to decipher the kaleidoscope of PTMs. Glycosylation and phosphorylation are important for many fundamental biological processes, and progress in their analysis by MS will be discussed. Further, paradigms for the application of proteomics to investigate complex mammalian signal transduction pathways will be presented (Session VII). The breath of this conference is well summarised in the two keynote talks by Peipei Ping (UCLA, USA) and Tony Pawson (Toronto, Canada). It is reaching across borders to integrate biological and clinical descriptive with mechanistic information. There is a prospering future for proteomics.

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