| Proteomics |
Website Links For Proteomics |
Information AboutProteomics |
| CATEGORIES ABOUT PROTEOMICS | |
| proteomics | |
| genomics | |
| bioinformatics | |
| proteins | |
| mass spectrometryproteomics | |
| genomics | |
| bioinformatics | |
| proteins | |
| mass spectrometry | |
| proteins | |
| genomics | |
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This technology is instrumental in Biomarker Discovery . The entirety of proteins in existence in an organism throughout its life cycle, or on a smaller scale the entirety of proteins found in a particular cell type under a particular type of stimulation, are referred to as the '' Proteome '' of the organism or cell type respectively. With completion of a rough draft of the Human genome, many researchers are now looking at how genes and proteins interact to form other proteins. A surprising finding of the Human Genome Project is that there are far fewer protein-coding genes in the human genome than there are proteins in the human proteome (~22,000 genes vs. ~400,000 proteins). The large increase in protein diversity is thought to be due to Alternative Splicing and Post-translational Modification of proteins. This discrepancy implies that protein diversity cannot be fully characterized by gene expression analysis alone, making proteomics a useful tool for characterizing cells and tissues of interest. To catalog all human proteins and ascertain their functions and interactions presents a daunting challenge for scientists. An international collaboration to achieve these goals is being co-ordinated by the Human Proteome Organisation ( HUPO ). BRANCHES OF PROTEOMICS # ''Protein separation''. All proteomic technologies rely on the ability to separate a complex mixture so that individual proteins are more easily processed with other techniques. # ''Protein identification''. Well-known methods include low-throughput sequencing through Edman degradation. Higher-throughput proteomic techniques are based on Mass Spectrometry , commonly Peptide Mass Fingerprinting on simpler instruments, or De Novo Repeat Detection sequencing on instruments capable of more than one round of mass spectrometry. Antibody-based assays can also be used, but are unique to one sequence motif. # ''Protein quantification''. Gel-based methods are used, including differential staining of gels with fluorescent dyes ( product. Additionally, these tools match spots between gels of similar samples to show, for example, proteomic differences between early and advanced stages of an illness. # ''Protein sequence analysis''. This is more of a bioinformatic branch, dedicated to searching databases for possible protein or peptide matches, but also functional assignment of domains, prediction of function from sequence, and evolutionary relationships of proteins. # ''Structural proteomics''. This concerns the high-throughput determination of protein structures in three-dimensional space. Common methods are X-ray Crystallography and NMR Spectroscopy . # ''Interaction proteomics''. This concerns the investigation of protein interactions on the atomic, molecular and cellular levels. see related article on Protein-protein Interaction Prediction . # ''Protein modification''. Almost all proteins are modified from their pure translated amino-acid sequence, so-called post-translational modification. Specialized methods have been developed to study phosporylation (phosphoproteomics) and glycosylation (glycoproteomics). # ''Cellular proteomics''. A new branch of proteomics. The goal is to map the location of proteins and protein-protein interactions in whole cells during key cell events. Centers around the use of techniques such as X-ray Tomography and optical fluorescence microscopy. KEY TECHNOLOGIES USED IN PROTEOMICS
PROTEIN DATABASES EXTERNAL LINKS
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