Abstract
Chemical modification is a powerful tool for investigating the accessibility and function of specific amino acids within folded proteins. It has provided significant information regarding the role of different amino acids at the binding sites of numerous enzymes and DNA binding proteins. This information has frequently been used to plan subsequent site-directed mutagenesis experiments. Additionally, the data from chemical modification experiments complements that from crystallographic and NMR data in elucidating the residues located at the DNA binding site.
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© 1994 Humana Press Inc.
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Plyte, S.E. (1994). Nitration of Tyrosine Residues in Protein-Nucleic Acid Complexes. In: Geoff Kneale, G. (eds) DNA-Protein Interactions. Methods in Molecular Biology™, vol 30. Humana Press. https://doi.org/10.1385/0-89603-256-6:151
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DOI: https://doi.org/10.1385/0-89603-256-6:151
Publisher Name: Humana Press
Print ISBN: 978-0-89603-256-9
Online ISBN: 978-1-59259-517-4
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