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Nature 446, 993-995 (26 April 2007) | doi:10.1038/446993a; Published online 25 April 2007
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Chemical biology: Dressed-up proteins
Gijsbert Grotenbreg1 & Hidde Ploegh1
Abstract
Proteins aren't just defined by their constituent amino acids — structural modifications can yield complex mixtures of protein forms. An approach that controls the addition of such modifications may help to define their role.
Polypeptides freshly minted from the cell's protein-assembly apparatus are by no means ready for active service. Both the peptide backbone and its side chains may need to be altered by post-translational modifications (PTMs), the covalent attachment of chemical groups that change the properties, and hence the function, of newly generated proteins.
- Gijsbert Grotenbreg and Hidde Ploegh are at the Whitehead Institute for Biomedical Research and the Department of Biology, Massachusetts Institute of Technology, 9 Cambridge Center, Cambridge, Massachusetts 02139, USA.
Email: ploegh@wi.mit.edu
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RESEARCH
Expanding the diversity of chemical protein modification allows post-translational mimicryNature Letters to Editor (26 Apr 2007)
