NMR spectroscopy articles within Nature

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  • 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 |

    Spectroscopic measurements of individual rare-earth ion electron spins are performed by detecting their microwave fluorescence, with the method coming close to practical single-electron spin resonance at millikelvin temperatures.

    • Z. Wang
    • , L. Balembois
    •  & E. Flurin
  • Article |

    Systematic alteration of HIV-1 TAR RNA and quantitative determination of its propensity to bind to the Tat protein establish a key role role for a rare and short-lived RNA state in Tat-dependent transactivation in cells.

    • Megan L. Ken
    • , Rohit Roy
    •  & Hashim M. Al-Hashimi
  • Article |

    Combining NMR spectroscopy-derived pseudocontact shifts (PCSs) with Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion enables protein structure determination of lowly populated high-energy states that are essential for macromolecular function.

    • John B. Stiller
    • , Renee Otten
    •  & Dorothee Kern
  • Article |

    Repression of a messenger RNA by a cognate microRNA depends not only on complementary base pairing, but also on the rearrangement of a single base pair, producing a conformation that fits better within the human Ago2 protein.

    • Lorenzo Baronti
    • , Ileana Guzzetti
    •  & Katja Petzold
  • Article |

    Chaperones interact with a canonical motif in α-synuclein, which can be prevented by phosphorylation of α-synuclein at Tyr39, whereas inhibition of this interaction leads to the localization of α-synuclein to the mitochondria and aggregate formation.

    • Björn M. Burmann
    • , Juan A. Gerez
    •  & Sebastian Hiller
  • Article |

    A high-affinity complex of histone H1 and prothymosin-α reveals an unexpected interaction mechanism, where the large opposite net charge enables the two proteins to remain highly disordered even in the complex.

    • Alessandro Borgia
    • , Madeleine B. Borgia
    •  & Benjamin Schuler
  • Letter |

    The intrinsically disordered CITED2 negative feedback regulator displaces the tightly bound hypoxia-inducible transcription factor HIF-1α from their common target TAZ1 through the formation of an intermediate ternary complex and thereby attenuates the hypoxic response.

    • Rebecca B. Berlow
    • , H. Jane Dyson
    •  & Peter E. Wright
  • Letter |

    Structural differences in 40- and 42-residue-long amyloid-β fibrils seeded in vitro from the cortical tissue of patients with different clinical subtypes of Alzheimer’s disease suggest that different fibril structures form in different disease variants and with different peptide lengths.

    • Wei Qiang
    • , Wai-Ming Yau
    •  & Robert Tycko
  • Letter |

    The structure of the core region of the mitochondrial calcium uniporter (MCU) is determined by NMR and electron microscopy, revealing that MCU is a homo-pentamer with a specific transmembrane helix forming a hydrophilic pore across the membrane, and representing one of the largest membrane protein structures characterized by NMR spectroscopy.

    • Kirill Oxenoid
    • , Ying Dong
    •  & James J. Chou
  • Letter |

    A small molecule, inhibitor of a protein–protein interaction between the transcription factor Pdr1 and the Med15 subunit of Mediator in the fungal pathogen Candida glabrata, is identified and characterized here; the compound iKIX1 inhibits Pdr1-mediated gene activation and resensitizes drug-resistant C. glabrata to azole antifungals in vitro and in animal models of disseminated and urinary tract infection.

    • Joy L. Nishikawa
    • , Andras Boeszoermenyi
    •  & Haribabu Arthanari
  • Letter |

    Although several X-ray crystal structures of G protein-coupled receptors (GPCRs) have been reported, relatively little is known about the conformational dynamics of these important membrane proteins; here, the authors used NMR spectroscopy to monitor the conformational changes that occur in the turkey β1-adrenergic receptor in the presence of antagonists, partial agonists, and full agonists.

    • Shin Isogai
    • , Xavier Deupi
    •  & Stephan Grzesiek
  • Article |

    Atomic resolution in-cell NMR and EPR spectroscopy show that the human amyloid protein α-synuclein remains disordered within all mammalian cells tested, including neurons, and identifies which parts of the protein dynamically interact or remain shielded from the cytoplasm, thus counteracting aggregation under physiological cell conditions.

    • Francois-Xavier Theillet
    • , Andres Binolfi
    •  & Philipp Selenko
  • Letter |

    NMR spectroscopy reveals the conformational changes of the μ-opioid receptor that are associated with receptor activation, helping to explain why the allosteric coupling between the agonist-binding pocket and the cytoplasmic G-protein-coupling interface of this receptor is relatively weak.

    • Rémy Sounier
    • , Camille Mas
    •  & Sébastien Granier
  • Article |

    dG•dT and rG•rU ‘wobble’ mispairs in DNA and RNA transiently form base pairs with Watson–Crick geometry via tautomerization and ionization with probabilities that correlate with misincorporation probabilities during replication and translation.

    • Isaac J. Kimsey
    • , Katja Petzold
    •  & Hashim M. Al-Hashimi
  • Letter |

    To prime reverse transcription of Moloney murine leukaemia virus, a transfer RNA molecule must bind two regions of the retroviral RNA, the primer binding site (PBS) and primer activation signal within the U5-PBS; here, the NMR structures of the U5-PBS RNA and tRNA primer are solved, with and without the retroviral nucleocapsid protein, which remodels these regions.

    • Sarah B. Miller
    • , F. Zehra Yildiz
    •  & Victoria M. D’Souza
  • Letter |

    A technique of NMR thermometry that relies on the inverse relationship between NMR linewidths and temperature can be used to map non-invasively the gas temperatures inside catalytic reactors, offering unprecedented capabilities for testing the approximations used in reactor modelling.

    • Nanette N. Jarenwattananon
    • , Stefan Glöggler
    •  & Louis-S. Bouchard
  • Outlook |

    Richard R. Ernst pioneered one- and two-dimensional nuclear magnetic resonance (NMR), and talks to Stephanie Harris about why dimensions are important in life as well as in science.

  • Article |

    RNAs undergo many types of post-transcriptional modification, including methylation of ribosomal RNAs; here the structure of the archaeal box C/D ribonucleoprotein complex bound to substrate RNA is determined, showing that the two methylation guide sequences exist in different contexts and revealing sequential regulation of methylation at the two sites.

    • Audrone Lapinaite
    • , Bernd Simon
    •  & Teresa Carlomagno
  • Letter |

    The structure of the oligomeric hepatitis C virus viroporin p7 protein, solved by NMR spectroscopy, is reported; this protein can self-assemble into a channel complex that conducts cations and has a funnel-like channel architecture.

    • Bo OuYang
    • , Shiqi Xie
    •  & James J. Chou
  • Article |

    This study develops an NMR-based approach that can capture previously inaccessible, highly transient, low-populated ‘excited states’ in RNA; the localized rearrangements in base-pairing giving rise to these states are found to affect function by changing the exposure of residues required for a specific biological process.

    • Elizabeth A. Dethoff
    • , Katja Petzold
    •  & Hashim M. Al-Hashimi
  • News & Views |

    Unpaired electrons can exert effects that allow interatomic contacts in molecules to be detected more easily using nuclear magnetic resonance. One such effect reveals unusual interactions between certain atoms in a protein.

    • Ivano Bertini
    •  & Claudio Luchinat
  • News & Views |

    The functions of proteins are critically coupled to their interplay with water, but determining the dynamics of most water molecules at protein surfaces hasn't been possible. A new spectroscopic method promises to change that.

    • Vincent J. Hilser
  • Letter |

    Templates are widely used to arrange molecular components so they can be covalently linked into complex molecules that are not readily accessible by classical synthetic methods. But, as larger structures are targeted, the synthesis of the templates themselves becomes challenging. It is now shown that 'molecular Verniers' can solve this problem: using a template with six binding sites and molecular building blocks with four porphyrins acting as binding sites, a 12-porphyrin nano-ring with a diameter of 4.7 nm is created. The ease and efficiency of this synthesis establishes Vernier templating as a powerful new strategy for producing large monodisperse macromolecules.

    • Melanie C. O’Sullivan
    • , Johannes K. Sprafke
    •  & Harry L. Anderson
  • News & Views |

    Nuclear magnetic resonance is a versatile analytical technique, but acquiring well-resolved NMR spectra of chemical surfaces has been hard. The coming of age of a spectral enhancement method should change all that.

    • Robert G. Griffin
  • Letter |

    The proteasome is a multi-protein complex that enzymatically degrades proteins. Proteolysis occurs in a barrel-shaped 20S core particle comprising three interconnected cavities, including a pair of antechambers in which substrates are held before degradation. These authors demonstrate that substrates interact actively with the antechamber walls and that the environment in this compartment is optimized to maintain the substrates in unfolded states so as to be accessible for hydrolysis.

    • Amy M. Ruschak
    • , Tomasz L. Religa
    •  & Lewis E. Kay
  • News Feature |

    Researchers in France have switched on the world's most powerful nuclear magnetic resonance instrument. Ananyo Bhattacharya asks whether it will attract new life to NMR spectroscopy.

    • Ananyo Bhattacharya