Post-Translational Modifications of Proteins

  • Radha G. Krishna
  • Finn Wold


The purpose of this chapter is to attempt to compile a list of the amino acid derivatives known to exist in proteins in a manner that may be of use to protein chemists concerned with protein sequencing and with the prediction and elucidation of the complete covalent structure of proteins. With the many reviews of the area of post-translational modifications of proteins written in the course of the last 15 years (Alix and Hays, 1983; Krishna and Wold, 1992; 1993; Uy and Wold, 1977; Whitaker, 1977; Wold, 1981; 1983), there is little justification for just another review; however, with the rapidly increasing use of mass spectrometry in the elucidation of protein structure (Biemann, 1992), and with mass spectrometry as the most obvious tool toward recognizing and identifying unusual amino acids in proteins, it has been suggested that a list of most of the known derivatives along with their molecular masses might be of some use, especially to the individuals at this meeting.


Mass Change Amino Acid Derivative Radical Mass Hexuronic Acid Texas Medical School 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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  1. Alix, J.-H. and Hayes, D., 1983 Why are macromolecules modified post-synthetically?, Biol. Cell 47:139.Google Scholar
  2. Biemann, K., 1992 Mass spectrometry of peptides and proteins. Ann. Rev. Biochem. 61:977.PubMedCrossRefGoogle Scholar
  3. Krishna, R. G. and Wold, F., 1992 Post-translational modifications: unique amino acids in proteins, in: Frontiers and New Horizons in Amino Acid Research, Takai, K., ed., Elsevier, Amsterdam.Google Scholar
  4. Krishna, R. G. and Wold, F., 1993 Post-translational modification of proteins. Adv. Enzymology and Related Areas of Mol. Biol. 67:in press.Google Scholar
  5. Stadtman, T. C., 1991 Biosynthesis and functioning of selenocysteine-containing enzymes, J. Biol. Chem. 266:16257.PubMedGoogle Scholar
  6. Uy, R. and Wold, F., 1977 Posttranslational covalent modification of proteins, Science 198:890.PubMedCrossRefGoogle Scholar
  7. Whitaker, J. R., 1977 in: Food Proteins, Improvement through Chemical and Enzymatic Modification, Feeney, R. E. and Whitaker, J. R., eds., Am. Chem. Soc., Washington DC.Google Scholar
  8. Wold, F., 1981 In vivo chemical modification of proteins, Ann. Rev. Biochem. 50:783.PubMedCrossRefGoogle Scholar
  9. Wold, F., 1983 Posttranslational protein modifications: perspectives and prospectives, in: Posttranslational Covalent Modifications of Proteins for Function, Johnson, C. B., ed., Academic Press, New York.Google Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Radha G. Krishna
    • 1
  • Finn Wold
    • 1
  1. 1.Department of Biochemistry and Molecular BiologyUniversity of Texas Medical SchoolHoustonUSA

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