Abstract
Synthetic peptides are used for many purposes in chemistry and biology. Among these, one of the most profitable has been the exploration of the specificity of proteolytic enzymes through quantitative studies of the enzymatic cleavage of sets of peptide substrates with systematic changes in specific positions. Similar information can be obtained when the inhibition of enzymatic activity by sets of peptides or peptide derivatives is studied; however, substrate studies have one major advantage in that the position of cleavage of a substrate peptide will always report on the orientation of the peptide in the active site. Inhibition might occur through the binding of peptides to different regions of the active site or, in extreme cases, through binding outside the active site.
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© 1994 Humana Press Inc., Totowa, NJ
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Dunn, B.M., Scarborough, P.E., Davenport, R., Swietnicki, W. (1994). Analysis of Proteinase Specificity by Studies of Peptide Substrates. In: Dunn, B.M., Pennington, M.W. (eds) Peptide Analysis Protocols. Methods in Molecular Biology, vol 36. Humana Press. https://doi.org/10.1385/0-89603-274-4:225
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DOI: https://doi.org/10.1385/0-89603-274-4:225
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