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Allosteric transition intermediates modelled by crosslinked haemoglobins.

Publication ,  Journal Article
Schumacher, MA; Dixon, MM; Kluger, R; Jones, RT; Brennan, RG
Published in: Nature
May 4, 1995

The structural end-points of haemoglobin's transition from its low-oxygen-affinity (T) to high-oxygen-affinity (R) state, have been well established by X-ray crystallography, but short-lived intermediates have proved less amenable to X-ray studies. Here we use chemical crosslinking to fix these intermediates for structural characterization. We describe the X-ray structures of three haemoglobins, alpha 2 beta 1S82 beta, alpha 2 beta 1Tm82 beta and alpha 2 beta 1,82Tm82 beta, which were crosslinked between the amino groups of residues beta Val1 and beta Lys82 by 3,3'-stilbenedicarboxylic acid (S) or trimesic acid (Tm) while in the deoxy state, and saturated with carbon monoxide before crystallization. alpha 2 beta 1S82 beta, which has almost normal oxygen affinity, is completely in the R-state conformation; however, alpha 2 beta 1Tm82 beta and alpha 2 beta 1,82Tm82 beta, both of which have low oxygen affinity, have been prevented from completing their transition into the R state and display many features of a transitional intermediate. These haemoglobins therefore represent a snapshot of the nascent R state.

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Published In

Nature

DOI

ISSN

0028-0836

Publication Date

May 4, 1995

Volume

375

Issue

6526

Start / End Page

84 / 87

Location

England

Related Subject Headings

  • Protein Conformation
  • Oxygen
  • Models, Molecular
  • Humans
  • Hemoglobins
  • General Science & Technology
  • Crystallography, X-Ray
  • Cross-Linking Reagents
  • Computer Graphics
  • Allosteric Regulation
 

Citation

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Schumacher, M. A., Dixon, M. M., Kluger, R., Jones, R. T., & Brennan, R. G. (1995). Allosteric transition intermediates modelled by crosslinked haemoglobins. Nature, 375(6526), 84–87. https://doi.org/10.1038/375084a0
Schumacher, M. A., M. M. Dixon, R. Kluger, R. T. Jones, and R. G. Brennan. “Allosteric transition intermediates modelled by crosslinked haemoglobins.Nature 375, no. 6526 (May 4, 1995): 84–87. https://doi.org/10.1038/375084a0.
Schumacher MA, Dixon MM, Kluger R, Jones RT, Brennan RG. Allosteric transition intermediates modelled by crosslinked haemoglobins. Nature. 1995 May 4;375(6526):84–7.
Schumacher, M. A., et al. “Allosteric transition intermediates modelled by crosslinked haemoglobins.Nature, vol. 375, no. 6526, May 1995, pp. 84–87. Pubmed, doi:10.1038/375084a0.
Schumacher MA, Dixon MM, Kluger R, Jones RT, Brennan RG. Allosteric transition intermediates modelled by crosslinked haemoglobins. Nature. 1995 May 4;375(6526):84–87.
Journal cover image

Published In

Nature

DOI

ISSN

0028-0836

Publication Date

May 4, 1995

Volume

375

Issue

6526

Start / End Page

84 / 87

Location

England

Related Subject Headings

  • Protein Conformation
  • Oxygen
  • Models, Molecular
  • Humans
  • Hemoglobins
  • General Science & Technology
  • Crystallography, X-Ray
  • Cross-Linking Reagents
  • Computer Graphics
  • Allosteric Regulation