Abstract
The most widely used applications for chemical modification are in primary structure analysis and in the identification of essential groups involved in the binding and catalytic sites of proteins. Chemical modifications, using an ever increasing number of cross-linkers, are involved in both protein “active center” identification (1), subunit cross-linking, protein-protein interaction, and many more (see http://www. piercenet. com/Technical/Docs/08/apps.pdf), and also in mapping the positions of disulfide linkage patterns in peptides containing tightly clustered cysteines (2). The methods discussed here are those used frequently in primary structure analysis.
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Carne, A.F. (2003). Chemical Modifications of Proteins as an Aid to Sequence Analysis. In: Smith, B.J. (eds) Protein Sequencing Protocols. Methods in Molecular Biology™, vol 211. Humana Press. https://doi.org/10.1385/1-59259-342-9:333
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DOI: https://doi.org/10.1385/1-59259-342-9:333
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