Abstract
Protein—protein interactions are required for nearly every cellular function and are therefore universally studied in biology. Traditionally such interactions have been identified and characterized by the means of biochemistry, and the power of this approach is certainly undisputed. However, besides the fact that in the “old days” the composition of protein complexes was mostly studied in vitro, the arsenal of biochemical methods is very effective for tight interactions only, especially those with slow off-rate kinetics. Protein purification protocols have substantial time requirements, which means that interactions of interest might simply not survive the isolation procedure. Chemical cross-linking, i.e. covalent tethering of proteins, can sometimes overcome this limitation but this is not a widely used method. This is partly due to the fact that specific cross-linking of proteins may not be feasible under relevant conditions, e.g. inside a cell.
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Kolanus, W. (1999). The Two Hybrid Toolbox. In: Famulok, M., Winnacker, EL., Wong, CH. (eds) Combinatorial Chemistry in Biology. Current Topics in Microbiology and Immunology, vol 243. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60142-2_3
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DOI: https://doi.org/10.1007/978-3-642-60142-2_3
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