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Post-Translational Modif ications of Proteins

  • Christoph Kannicht
  • Birte Fuchs
Protocol
  • 3.1k Downloads
Part of the Springer Protocols Handbooks book series (SPH)

1. Introduction

Post-translational modifications (PTMs) of proteins are referred to as chemical modifications or cleavage of the protein after its translation. The protein's polypeptide chain may be altered by proteolytic cleavage, formation of disulfide bonds or covalent attachment of phosphate, sulfate, alkyl groups, lipids, carbohydrates, polypeptides, and others (1,2). Though some covalent modifications, e.g., N-glycosylation, occur cotranslationally at the nascent polypeptide chain, the term “post-translational modifications” is commonly used to cover both, co- and post-translational modifications, for reasons of simplicity. The majority of all proteins undergo PTMs: For example around 30% of all proteins found in a mammalian cell exist in a phosphorylated state, and nearly all circulating plasma proteins are glycosylated.

PTMs can influence charge, hydrophobicity, conformation, immunological properties, stability, turnover, localization, and activity of a protein (3,4). The...

Keywords

Electron Capture Dissociation Electron Detachment Dissociation Free Cysteine Residue Common Core Structure Tryptic Protein Digestion 
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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Copyright information

© Humana Press, a part of Springer Science+Business Media, LLC 2008

Authors and Affiliations

  • Christoph Kannicht
    • 1
  • Birte Fuchs
    • 1
  1. 1.Institut fur Molekularbiologie and BiochemiFreie Universitat BerlinBerlinGermany

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