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Related Experiment Videos

Flexibility and nucleation in sickle hemoglobin.

M Ivanova1, R Jasuja, L Krasnosselskaia

  • 1Department of Physics, Drexel University, Philadelphia, PA 19104, USA.

Journal of Molecular Biology
|December 6, 2001
PubMed
Summary

Hemoglobin C-Harlem self-assembles into crystals, unlike sickle hemoglobin fibers. This crystal formation involves significantly suppressed nucleation, suggesting altered molecular interactions in this double mutant hemoglobin.

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A model for the sickle hemoglobin fiber using both mutation sites.

Protein science : a publication of the Protein Society·2000

Area of Science:

  • Biophysics
  • Molecular Biology
  • Hematology

Background:

  • Sickle hemoglobin (HbS) forms fibers, causing sickle cell disease.
  • Hemoglobin C-Harlem (HbC-Harlem) is a double mutant with distinct structural properties.
  • Understanding hemoglobin self-assembly is crucial for disease mechanism insights.

Purpose of the Study:

  • To investigate the self-assembly mechanism of Hemoglobin C-Harlem (HbC-Harlem).
  • To compare the assembly pathway and kinetics of HbC-Harlem with HbS.
  • To elucidate the structural basis for observed differences in assembly.

Main Methods:

  • Electron microscopy (EM) for structural analysis.
  • Fourier transforms for unit cell parameter determination.
  • Differential interference contrast (DIC) microscopy and birefringence.

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  • Solubility measurements using a photolytic micromethod.
  • Assembly kinetics analysis via photolysis of carbon monoxide derivative.

    • Main Results:

    • HbC-Harlem forms crystals, distinct from HbS fibers, with identical unit cell parameters.
    • Assembly kinetics show exponential growth with stochastically distributed onset times.
    • Nucleation (homogeneous and heterogeneous) is suppressed by ~11 orders of magnitude compared to HbS.
    • Solubility is similar to HbS fibers, despite different assembly structures.

    Conclusions:

    • HbC-Harlem self-assembly follows a nucleation-dependent process, similar to HbS.
    • Suppressed nucleation in HbC-Harlem is attributed to increased contact energy and decreased vibrational entropy.
    • These factors explain the formation of linear double-strands and crystal structures.