Protein structure predictions articles within Nature

Featured

  • Article |

    A computational model generates conformational ensembles of 28,058 intrinsically disordered proteins and regions (IDRs) in the human proteome and sheds light on the relationship between sequence, conformational properties and functions of IDRs.

    • Giulio Tesei
    • , Anna Ida Trolle
    •  & Kresten Lindorff-Larsen

  • Article
    | Open Access

    An analysis of the evolutionary distribution of predicted structures for the metamorphic protein KaiB using AF-Cluster reveals that both conformations of KaiB were distributed in clusters across the KaiB family.

    • Hannah K. Wayment-Steele
    • , Adedolapo Ojoawo
    •  & Dorothee Kern

  • Article
    | Open Access

    AlphaFold is used to predict the structures of almost all of the proteins in the human proteome—the availability of high-confidence predicted structures could enable new avenues of investigation from a structural perspective.

    • Kathryn Tunyasuvunakool
    • , Jonas Adler
    •  & Demis Hassabis

  • Article
    | Open Access

    AlphaFold predicts protein structures with an accuracy competitive with experimental structures in the majority of cases using a novel deep learning architecture.

    • John Jumper
    • , Richard Evans
    •  & Demis Hassabis

  • Article |

    AlphaFold predicts the distances between pairs of residues, is used to construct potentials of mean force that accurately describe the shape of a protein and can be optimized with gradient descent to predict protein structures.

    • Andrew W. Senior
    • , Richard Evans
    •  & Demis Hassabis

  • Article |

    A massively parallel computational and experimental approach for de novo designing and screening small hyperstable proteins targeting influenza haemagglutinin and botulinum neurotoxin B identifies new therapeutic candidates more robust than traditional antibody therapies.

    • Aaron Chevalier
    • , Daniel-Adriano Silva
    •  & David Baker

  • Letter |

    In this study, 83 proteins containing helix–loop–helix–loop repeats were designed—with sequences unrelated to known repeat proteins—and experimentally characterized; 43 solution X-ray scattering spectra and 15 structures of the designed proteins show that these non-natural repeat proteins have a broad range of curvatures and that their overall structures are in close agreement with design models.

    • TJ Brunette
    • , Fabio Parmeggiani
    •  & David Baker

  • Letter |

    Predicting the structure of a folded protein from first principles for any given amino-acid sequence remains a formidable computational challenge. To recruit human abilities to the task, these authors turned their Rosetta structure prediction algorithm into an online multiplayer game in which thousands of non-scientists competed and collaborated to produce new algorithms and search strategies for protein structure refinement. This shows that computationally complex problems can be effectively 'crowd-sourced' through interactive multiplayer games.

    • Seth Cooper
    • , Firas Khatib
    •  & Foldit players

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