Protein interaction mapping

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D) polyacrylamide gels. These types of experiments have been performed for more than twenty years to build databases of proteins expressed from certain cell or tissue types (Anderson and Anderson, 1996 O Farrell, 1975). Although this remains an important component of proteomics research, the field has expanded due to the development of additional technologies. Proteomics can be broadly divided into two areas of research (i) protein expression mapping, and (ii) protein interaction mapping. 

Use of mass spectrometry for protein-protein interaction mapping... 

The experiments described above indicate that technology is available to couple SPR with mass spectrometry. These methods should be useful for protein-protein interaction mapping. For example, immobilized proteins can be used as hooks for fishing binding partners from complex protein mixtures under native conditions. The coupling of techniques can lead not only to the rapid identification of interacting proteins but will also provide information on the kinetic parameters of the interaction. This approach should serve as an excellent complement to the use of in vivo techniques such as the yeast two-hybrid system. 

Enright, A. J., Iliopoulos, I., Kyrpides, N. C., andOuzounis, C. A. (1999). Protein interaction maps for complete genomes based on gene fusion events. Nature 402, 86-90. 

As well as protein expression analysis, proteomics in its broadest sense also includes protein-protein interaction mapping. This can range from small studies using a single protein or peptide to fish ouf any proteins that interact with it... 

Legrain P et al. Genome-wide protein interaction maps using two-hybrid systems. FEBS Lett 2000 480 32-36. 

Rain J-C et al. The protein-protein interaction map of Helicobacter pylori. Nature 2001 409 211-215. 

Walhout AJM et al. Protein interaction mapping in C.elegans using proteins involved in vulval development. Science 2000 287 116-122. 

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