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The complete genome sequence of many organisms is now available. Many novel genes have been identified from the sequence analysis; however, their functions are unclear. The challenge of understanding of the function of each gene in the genome has led to the development of large scale, high throughput experimental techniques collectively known as functional genomics. Proteomics is a branch of functional genomics for large scale study of protein properties, such as expression levels, post translational modifications and interaction with other molecules to obtain a global view of cellular process in the protein level.
Proteomics is a relative new, challenging and fast developing field. The proteome is not a static but a dynamic feature of an organism; it depends on location of a tissue and changes constantly in response to internal and external stimuli. There are various ways a gene can be spliced in constructing mRNA, and posttranslational modifications can occur to any protein. These make human beings to have somewhere between 200,000 and 1 million proteins instead of an estimated 30,000 to 40,000 genes. The dynamic concentration of these proteins varies in several orders of magnitude. In addition, unlike genes, proteins vary widely in their chemical behaviors, making it difficult to come up with one technique that works equally well on all proteins. Therefore, proteomic analysis requires sampling, separation and concentration, identification, structural characterization and protein-protein interaction network determination and rigorous bioinformatics analysis.
We do not have a way of amplifying protein in analogue with the PCR techniques in DNA analysis. Therefore, we need ultra high sensitive detection techniques for proteome analysis. Mass spectrometry (MS) is an important analytical technique for molecular structure characterization because of its high sensitivity (10-18 mole), specificity (peptide mass fingerprinting, sequence tag and post-translational modification determination) and speed (analysis of whole proteome in a day). Mass spectrometry coupled with protein separation using 2D-PAGE or multidimensional liquid chromatography is the currently technologies for proteomics. This technology can generate huge amount of raw mass spectra and/or tandem mass spectra. These MS data would be analyzed by bioinformatics tools for the rapid retrieval of known proteins from protein databases, and the identification of novel proteins whose functions are hitherto unknown.
On the basis of the above, it is obvious that the quality/reliability of the MS data and their mode of analysis and data mining methods by bioinformatics are extremely important in the correct identification and characterization of proteins from the existing protein database such as SWISS-Prot etc. With the initiation of several proteome projects such as the plasma, liver, and brain proteome projects at the international level but coordinated by the Human Proteome Organization (HUPO), it is important to lay the ground rules in sample preparation, data collection, and data analysis for all participating laboratories. In this workshop we wish to examine and discuss some of the problems existing in data analysis and data mining in proteomics through a series of seminars and discussion papers given by eminent international and local speakers.
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Please complete the registration form (MSWord|PDF|PS) and fax to (65) 6873 8292 or email to ims@nus.edu.sg.
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