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Journal Article · Nature · 2026Cover article

Cryo-EM structures of a haemoglobin variant reveal a new allosteric state

P. Natarajan, D. Okafor, L. Fischer, A. Rao

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Cited by 3

Abstract

Haemoglobin switches between two shapes as it binds oxygen. Using cryo-EM of a disease-causing variant, we capture a third, intermediate state, and show how a small molecule can stabilise it to improve oxygen delivery.

Cite

P. Natarajan, D. Okafor, L. Fischer, A. Rao (2026). Cryo-EM structures of a haemoglobin variant reveal a new allosteric state. Nature. https://doi.org/10.5555/demo.2026.001

BibTeX
@article{natarajan2026cryo,
  title = {Cryo-EM structures of a haemoglobin variant reveal a new allosteric state},
  author = {P. Natarajan and D. Okafor and L. Fischer and A. Rao},
  journal = {Nature},
  year = {2026},
  doi = {10.5555/demo.2026.001},
  url = {https://doi.org/10.5555/demo.2026.001},
  abstract = {Haemoglobin switches between two shapes as it binds oxygen. Using cryo-EM of a disease-causing variant, we capture a third, intermediate state, and show how a small molecule can stabilise it to improve oxygen delivery.}
}

Download BibTeXDownload RIS (EndNote, Zotero, Mendeley)DOI: 10.5555/demo.2026.001

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