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Identification of Posttranslational Modifications in Neuropeptides

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Part of the book series: Experimental Biology and Medicine ((EBAM,volume 14))

Abstract

Protein sequence data is now being deduced from cDNA sequences at rates which exceed the capacity of protein chemists to analyze post-translational processing events. Proteins may undergo a large number of post-translational modifications including glycosylation, phosphorylation, proteolytic processing, and disulfide bond formation, among many others (1). At present it is not possible to predict, with accuracy, which post-translational modifications of a particular protein sequence might occur. Principal factors determining post-translational events include primary structure, but higher orders of structure also appear to be important (2). Tissue-specific expression of the processing enzymes is also important (3–5). If the ultimate structure of a gene product is to be determined, it is necessary to purify the proteins or peptides in question and to determine their structures directly.

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© 1987 Springer Science+Business Media New York

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Dixon, J.E., Yazdanparast, R., Smith, D., Andrews, P.C. (1987). Identification of Posttranslational Modifications in Neuropeptides. In: Walsh, K.A. (eds) Methods in Protein Sequence Analysis · 1986. Experimental Biology and Medicine, vol 14. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-480-1_41

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  • DOI: https://doi.org/10.1007/978-1-59259-480-1_41

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-4757-5826-9

  • Online ISBN: 978-1-59259-480-1

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