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. 1967 Jul;58(1):19–26. doi: 10.1073/pnas.58.1.19

Spin-label study of hemoglobin conformations in solution.

S Ogawa, H M McConnell
PMCID: PMC335590  PMID: 4292100

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BENESCH R. E., BENESCH R. The influence of oxygenation on the reactivity of the--SH groups of hemoglobin. Biochemistry. 1962 Sep;1:735–738. doi: 10.1021/bi00911a002. [DOI] [PubMed] [Google Scholar]
  2. BUCCI E., FRONTICELLI C., CHIANCONE E., WYMAN J., ANTONINI E., ROSSI-FANELLI A. THE PROPERTIES AND INTERACTIONS OF THE ISOLATER ALPHA AND BETA CHAINS OF HUMAN HAEMOGLOBIN. I. SEDIMENTATION AND ELECTROPHORETIC BEHAVIOUR. J Mol Biol. 1965 May;12:183–192. doi: 10.1016/s0022-2836(65)80292-3. [DOI] [PubMed] [Google Scholar]
  3. KENDREW J. C. Myoglobin and the structure of proteins. Science. 1963 Mar 29;139(3561):1259–1266. doi: 10.1126/science.139.3561.1259. [DOI] [PubMed] [Google Scholar]
  4. Koshland D. E., Jr, Némethy G., Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry. 1966 Jan;5(1):365–385. doi: 10.1021/bi00865a047. [DOI] [PubMed] [Google Scholar]
  5. MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
  6. MUIRHEAD H., PERUTZ M. F. STRUCTURE OF HAEMOGLOBIN. A THREE-DIMENSIONAL FOURIER SYNTHESIS OF REDUCED HUMAN HAEMOGLOBIN AT 5-5 A RESOLUTION. Nature. 1963 Aug 17;199:633–638. doi: 10.1038/199633a0. [DOI] [PubMed] [Google Scholar]
  7. McConnell H. M., Boeyens J. C. Spin-label determination of enzyme symmetry. J Phys Chem. 1967 Jan;71(1):12–14. doi: 10.1021/j100860a002. [DOI] [PubMed] [Google Scholar]
  8. Ohnishi S., Boeyens J. C., McConnell H. M. Spin-labeled hemoglobin crystals. Proc Natl Acad Sci U S A. 1966 Sep;56(3):809–813. doi: 10.1073/pnas.56.3.809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. PERUTZ M. F. Relation between structure and sequence of haemoglobin. Nature. 1962 Jun 9;194:914–917. doi: 10.1038/194914a0. [DOI] [PubMed] [Google Scholar]
  10. Pauling L., Coryell C. D. The Magnetic Properties and Structure of Hemoglobin, Oxyhemoglobin and Carbonmonoxyhemoglobin. Proc Natl Acad Sci U S A. 1936 Apr;22(4):210–216. doi: 10.1073/pnas.22.4.210. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Perutz M. F., Mathews F. S. An x-ray study of azide methaemoglobin. J Mol Biol. 1966 Oct 28;21(1):199–202. doi: 10.1016/0022-2836(66)90088-x. [DOI] [PubMed] [Google Scholar]
  12. RIGGS A. The binding of N-ethylmaleimide by human hemoglobin and its effect upon the oxygen equilibrium. J Biol Chem. 1961 Jul;236:1948–1954. [PubMed] [Google Scholar]
  13. ROSSIFANELLI A., ANTONINI E., CAPUTO A. HEMOGLOBIN AND MYOGLOBIN. Adv Protein Chem. 1964;19:73–222. doi: 10.1016/s0065-3233(08)60189-8. [DOI] [PubMed] [Google Scholar]
  14. Rosemeyer M. A., Huehns E. R. On the mechanism of the dissociation of haemoglobin. J Mol Biol. 1967 Apr 28;25(2):253–273. doi: 10.1016/0022-2836(67)90141-6. [DOI] [PubMed] [Google Scholar]
  15. Stone T. J., Buckman T., Nordio P. L., McConnell H. M. Spin-labeled biomolecules. Proc Natl Acad Sci U S A. 1965 Oct;54(4):1010–1017. doi: 10.1073/pnas.54.4.1010. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Watts-Tobin R. J. The oxidation of haemoglobin. J Mol Biol. 1967 Feb 14;23(3):305–322. doi: 10.1016/s0022-2836(67)80107-4. [DOI] [PubMed] [Google Scholar]

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