Abstract
To help maintain their three-dimensional structure, many proteins contain disulfide bridges between cysteine residues. Cysteine residues can cause problems during Edman sequence analysis, and quantification of cysteine and cystine by amino acid analysis is difficult since these residues are unstable during acid hydrolysis.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Glazer, A. N., Delange, R. J., and Sigman, D. S. (1975) Chemical characterization of proteins and their derivatives, in Chemical Modifications of Proteins (Work, T. S and Work. E., eds.), North Holland, Amsterdam, 21–24.
Allen, G. (1989) Sequencing of proteins and peptides, in Laboratory Techniques in Biochemistry and Molecular Biology (Burdon, R. H. and Van Knippenberg, P. H., eds.), Elsevier, Amsterdam.
Vestling, M. M., Kelly, M. A., and Fenselau, C. (1994) Optimisation by mass spectrometry of a tryptophan-specific protein cleavage reaction. Rapid Commun. Mass Spectrom. 8, 786–790.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Humana Press Inc., Totowa, NJ
About this protocol
Cite this protocol
Ward, M. (1996). Pyridylethylation of Cysteine Residues. In: Walker, J.M. (eds) The Protein Protocols Handbook. Springer Protocols Handbooks. Humana Press. https://doi.org/10.1007/978-1-60327-259-9_54
Download citation
DOI: https://doi.org/10.1007/978-1-60327-259-9_54
Publisher Name: Humana Press
Print ISBN: 978-0-89603-338-2
Online ISBN: 978-1-60327-259-9
eBook Packages: Springer Book Archive