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Chemical biology

Dressed-up proteins

Nature volume 446, pages 994–995 (2007)Cite this article

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. PTMs also control the degradation of aberrant proteins and those at the end of their lifespan. Such modifications dramatically expand the compositional and functional complexity of these molecules. Not satisfied with leaving everything to nature's whim, chemists are taking great strides in developing PTM-mimics. On page 1105 of this issue1, van Kasteren et al. describe strategies that offer precise control over the attachment of carbohydrates and other PTM-mimics to polypeptides.

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Figure 1: Dressing up proteins.

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Authors and Affiliations

  1. 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. ploegh@wi.mit.edu,

    Gijsbert Grotenbreg & Hidde Ploegh

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  1. Gijsbert Grotenbreg
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  2. Hidde Ploegh
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Grotenbreg, G., Ploegh, H. Dressed-up proteins. Nature 446, 994–995 (2007). https://doi.org/10.1038/446993a

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