Proteins are biopolymers of amino acids (polypeptides), joined by peptide bonds, that are generated by ribosomes. The amino acid sequence, encoded by its gene, determines a protein’s structure and function. Newly synthesized proteins can be modified by post-translational modification, altering its protein folding, stability and activity. Proteins often associate into protein–protein interaction networks for function.


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News and Comment

  • News and Views |

    Hydrogenases are very powerful biocatalysts for dihydrogen cleavage. Now, X-ray crystallography shows how [Fe]-hydrogenase requires ligand exchanges at the metal centre and significant molecular motions to open and close its active site to effectively transfer a hydride to an electrophilic organic substrate.

    • Yvain Nicolet
    Nature Catalysis 2, 481-482
  • News and Views |

    The concept that resistance against androgen receptor (AR) signalling inhibitors is explained by AR variants (ARVs) has spread as a seductive meme. However, two problems have delayed the translation of these findings to clinical practice: the complexity of the mechanism of action and the challenging development of clinical decision-making tools involving ARVs.

    • Florian Handle
    •  & Frank Claessens
  • News and Views |

    The advent of PROTACs that degrade the entire protein target rather than simply inhibiting it bring druggable yet apparently non-functional binding sites into play for medicinal chemists to do their work.

    • Dafydd Owen
  • News and Views |

    Centromere identity must be maintained through multiple generations. A new study reveals a Constitutive Centromere-Associated Network (CCAN)-dependent retention of CENP-A, a key epigenetic mark for centromeres, in centromeres during DNA replication and a replication-dependent error correction to eliminate ectopic CENP-A in chromosome arms.

    • Masatoshi Hara
    •  & Tatsuo Fukagawa
    Nature Cell Biology 21, 669-671