Protein folding

Protein folding is the process by which proteins achieve their mature functional (native) tertiary structure, and often begins co-translationally. Protein folding requires chaperones and often involves stepwise establishment of regular secondary and supersecondary structures, namely α-helices and β-sheets, that fold rapidly, stabilized by hydrogen bonding and disulphide bridges, and then tertiary structure.

Latest Research and Reviews

News and Comment

  • News and Views |

    Thermodynamic principles are used to map the phase behavior of a tunable protein-binding system under crowded cellular conditions. This study marks a substantial step forward in relating molecular interactions to material properties and cellular processes involving protein self-assembly.

    • Roshan Mammen Regy
    •  & Jeetain Mittal
  • News and Views |

    A new molecule that specifically activates a key protein homeostasis pathway has been identified. The ability to initiate the IRE1–XBP1s branch of the unfolded protein response opens up new avenues for basic research and treatment of disease.

    • Nadia Cummins
    •  & Rebecca C. Taylor
    Nature Chemical Biology 16, 1038-1039
  • News and Views |

    Secretory proteins undergo multiple rounds of co- and post-translational quality control checks inside the cell, but how their integrity is maintained outside the cell is an emerging topic. A study establishes a model system to investigate how the extracellular proteome is protected and integrates its findings into existing immune pathways.

    • Brant M. Webster
    • , Holly K. Gildea
    •  & Andrew Dillin
    Nature Cell Biology 22, 911-912
  • News and Views |

    A new study reveals that, in addition to its longstanding role in recruiting proteins to the proteasome, ubiquitination can also induce a structural destabilization that allows the target protein to be efficiently unraveled for degradation.

    • Cameron G. Roberts
    •  & Jonathan N. Pruneda