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Related Experiment Videos

Conformational changes in the hemoglobin S system as seen by proton binding

H P Scholberg, C Fronticelli, E Bucci

    The Journal of Biological Chemistry
    |September 25, 1980
    PubMed
    Summary

    Hemoglobin S exhibits altered proton binding due to a histidine at beta 2, potentially forming a salt bridge with glutamate 7. This structural change may influence hemoglobin fiber formation.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Hemoglobin S causes sickle cell disease due to altered protein structure.
    • Understanding proton binding is crucial for hemoglobin function.

    Purpose of the Study:

    • To investigate the proton binding behavior of hemoglobin S and A derivatives.
    • To identify the molecular basis of altered protonation in hemoglobin S.

    Main Methods:

    • Proton binding measurements on carbon monoxy hemoglobins A and S.
    • Analysis of beta-subunits and beta (1-55) peptides.
    • Proton nuclear magnetic resonance (NMR) spectroscopy.

    Main Results:

    • Hemoglobin S systems show a significant shift in pK values for a specific group.
    • The pK shifts from ~7.0 to 8.35 in modified beta-subunits and >9.0 in beta (1-55) peptides.
    • NMR identified histidine at beta 2 in the beta (1-55) peptide from hemoglobin S as the affected residue.

    Conclusions:

    • A salt bridge between beta 2 Histidine and beta 7 Glutamate is proposed in hemoglobin S.
    • This interaction likely disrupts the A helix structure in beta-subunits.
    • Stabilization of this structure via extramolecular contacts may be key to hemoglobin S fiber formation.

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