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Sulphydryl groups as a new molecular probe at the α1β1 interface in haemoglobin using Fourier transform infrared spectroscopy

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Abstract

THE haemoglobin molecule consists of a pair of subunits, each of which is made up of two different haem-bearing polypeptide chains, α and β. The contacts betwen the two αβ subunit pairs are not covalent and constitute the α1β2, (and α2β1) interface. Symmetrical dissociation1 of the haemoglobin molecule occurs relatively easily at this interface. Large changes in the α1β2 contacts occur2 as the molecule switches from the T to the R conformation during ligand binding3.

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Authors and Affiliations

  1. Departments of Physiological Chemistry and Medicine, Ohio State University College of Medicine, Columbus, Ohio, 43210

    JAMES O. ALBEN, GEORGE H. BARE & PHILIP A. BROMBERG

Authors
  1. JAMES O. ALBEN
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  2. GEORGE H. BARE
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  3. PHILIP A. BROMBERG
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ALBEN, J., BARE, G. & BROMBERG, P. Sulphydryl groups as a new molecular probe at the α1β1 interface in haemoglobin using Fourier transform infrared spectroscopy. Nature 252, 736–738 (1974). https://doi.org/10.1038/252736a0

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  • DOI: https://doi.org/10.1038/252736a0

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