Molecular conformation articles from across Nature Portfolio

Molecular conformation is any spatial arrangement of the atoms in a molecule which can be interconverted by rotations about formally single bonds. Biopolymers, such as polynucleotides, polypeptides or polysaccharides, may change conformation in response to changes in their environment.


Latest Research and Reviews

News and Comment

  • News & Views |

    Complexity is a hallmark of biological systems, but scientific experiments are typically conducted in simplified conditions. Now, diverse polymers that mimic the local environments of complex biological mixtures have been shown to improve protein folding, stability and function.

    • Alana P. Gudinas
    •  & Danielle J. Mai
    Nature Chemistry 15, 751-752
  • News & Views |

    Although critically important for protein function, post-translational modifications are complex and notoriously difficult to study. Now, the effects of O-GlcNAcylation on chaperone activity and the accompanying inhibition of amyloid fibril formation have been revealed, potentially yielding new routes to combat neurodegeneration.

    • Sheena E. Radford
    •  & Theodoros K. Karamanos
    Nature Chemistry 13, 397-399
  • News & Views |

    The crystal structure of an oligosaccharyltransferase in complex with a sugar donor and an acceptor peptide provides insight into the mechanism of protein glycosylation and reveals how lipid-linked oligosaccharides are positioned in the enzyme active site.

    • Shiteshu Shrimal
    • , Natalia A Cherepanova
    •  & Reid Gilmore
  • Research Highlights |

    Membrane transporter proteins are critical for cellular uptake and export of molecules, and are reported to function by a number of different molecular mechanisms. The new occluded state structure of the uracil transporter, UraA, from Escherichia coli, reveals that both coordinated movement of the two domains of a single protomer together with dimer formation are important for transport activity.

    • Bernadette Byrne
    Cell Research 27, 965-966
  • Research Highlights |

    Although energy-dependent protein destruction by the proteasome has been known for over 30 years, how this intricate molecular machine uses ATP to power protein degradation has remained very poorly understood. In a recently published paper, Ding et al. present a snapshot of the proteasome mid-catalysis, yielding new and unexpected insights into the catalytic mechanism of this ATP-powered multisubunit machine.

    • Robert J Tomko Jr
    Cell Research 27, 307-308