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Conformational interconversion in protein crystals.

L Zhu1, J T Sage, A A Rigos

  • 1Department of Physics, Northeastern University, Boston, MA 02115.

Journal of Molecular Biology
|March 5, 1992
PubMed
Summary
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Lowering pH alters carbonmonoxy myoglobin crystal structure, shifting the distal pocket between closed and open states. Crystal packing slows conformational changes compared to solution.

Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Myoglobin's distal pocket conformation influences its function.
  • Carbonmonoxy myoglobin (MbCO) exhibits distinct structural states.
  • Raman spectroscopy is sensitive to Fe-CO bond vibrations and protein structure.

Purpose of the Study:

  • To investigate the effect of pH on carbonmonoxy myoglobin crystal structure.
  • To characterize the conformational changes in the distal pocket of MbCO crystals.
  • To compare conformational dynamics in solution versus crystalline states.

Main Methods:

  • Raman spectroscopy to monitor Fe-CO modes and globin unfolding.
  • Laser photolysis to induce and quantify conformational changes.
  • pH variation (7 to 4) to induce structural transitions.

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Main Results:

  • Lowering pH from 7 to 4 induced a structural change in MbCO crystals, associated with Fe-CO Raman modes at 508 and 491 cm-1.
  • This change corresponds to a transition from a 'closed' to an 'open' distal pocket conformation.
  • Conformational interconversion rates were significantly slower in crystals than in solution, indicating increased energy barriers due to crystal packing.

Conclusions:

  • The distal pocket of carbonmonoxy myoglobin crystals can adopt distinct conformations influenced by pH.
  • Crystal packing restricts conformational dynamics compared to aqueous solution.
  • Further X-ray and neutron diffraction studies are needed to elucidate the precise structural details of these pH-dependent conformational states.