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Is apomyoglobin a molten globule? Structural characterization by NMR

D Eliezer1, P E Wright

  • 1Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Journal of Molecular Biology
|November 8, 1996
PubMed
Summary

Sperm whale apomyoglobin exhibits a well-defined, holomyoglobin-like structure, except for a flexible region prone to conformational fluctuations. This protein displays native characteristics, differing from the classical molten globule model.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Apomyoglobin, the protein without its heme group, is crucial for understanding myoglobin's structure-function relationship.
  • Investigating apomyoglobin's native state provides insights into protein folding and dynamics.

Purpose of the Study:

  • To elucidate the three-dimensional structure and dynamics of recombinant sperm whale apomyoglobin in its native state.
  • To compare the structural features of apomyoglobin with its holoprotein counterpart.

Main Methods:

  • Multi-dimensional heteronuclear Nuclear Magnetic Resonance (NMR) spectroscopy was employed.
  • Isotopically labeled (15N, 13C) apomyoglobin was used for resonance assignment.

Main Results:

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  • Resonance assignments for backbone amides (1HN, 15N) and alpha-carbons (13Calpha) were obtained for a significant portion of the apomyoglobin.
  • Observed chemical shifts indicate secondary structures nearly identical to carbonmonoxy-holomyoglobin.
  • A specific region (EF loop, F helix, FG loop, G helix) showed broadened resonances, suggesting conformational flexibility.

Conclusions:

  • Apomyoglobin largely adopts a stable, holomyoglobin-like structure in solution.
  • Conformational fluctuations in a specific region suggest dynamic exchange between folded and unfolded states.
  • Apomyoglobin displays characteristics of a native globular protein, not a classical molten globule.