Working paper
Origin of complexity in haemoglobin evolution
- Abstract:
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Most proteins associate into multimeric complexes with specific architectures1,2, which often have functional properties such as cooperative ligand binding or allosteric regulation3. No detailed knowledge is available about how any multimer and its functions arose during evolution. Here we use ancestral protein reconstruction and biophysical assays to elucidate the origins of vertebrate haemoglobin, a heterotetramer of paralogous α- and β-subunits that mediates respiratory oxygen transport an...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
-
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(Other, Accepted manuscript, 30.5KB)
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(Accepted manuscript, 58.2MB)
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- Publisher copy:
- 10.1038/s41586-020-2292-y
Authors
Funding
Bibliographic Details
- Publisher:
- Springer Nature Publisher's website
- Host title:
- Nature
- Volume:
- 581
- Issue:
- 7809
- Pages:
- 480-485
- Publication date:
- 2020-05-20
- DOI:
- EISSN:
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1476-4687
- ISSN:
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0028-0836
Item Description
- Language:
- English
- Pubs id:
-
1088032
- Local pid:
- pubs:1088032
- Deposit date:
- 2020-06-25
Terms of use
- Copyright holder:
- Pillai et al.
- Copyright date:
- 2020
- Rights statement:
- © The Authors, under exclusive licence to Springer Nature Limited 2020
- Notes:
-
This is the accepted manuscript version of the article. The final version is available online from Springer Nature at https://doi.org/10.1038/s41586-020-2292-y
Note: An author correction exists for this article, originally published and available at: https://doi.org/10.1038/s41586-020-2472-9
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