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Flexibility in crystalline insulins.

J Badger1

  • 1Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254.

Biophysical Journal
|March 1, 1992
PubMed
Summary
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Structural changes in insulin due to crystal contacts are localized, unlike T4 lysozyme. These protein structure alterations involve local atomic repacking, not rigid domain shifts, highlighting short-range interactions in protein flexibility.

Area of Science:

  • Structural biology
  • Protein crystallography
  • Biophysics

Background:

  • Protein structure flexibility can be influenced by crystal packing environments.
  • Previous studies on T4 lysozyme showed domain movements in different crystal forms.
  • Understanding atomic-level changes is crucial for interpreting protein crystal structures.

Purpose of the Study:

  • To compare atomic displacements in two crystal forms of insulin.
  • To investigate how crystal contacts affect protein structure at the atomic level.
  • To determine if structural changes propagate through the insulin molecule.

Main Methods:

  • Comparison of atomic coordinates from two crystal structures of insulin.
  • Analysis of atomic displacements and repacking of amino acid residues.

Related Experiment Videos

  • Evaluation of the propagation of structural changes through the protein core.

    • Main Results:

    • Structural changes in insulin were confined to local amino acid residues near crystal contacts.
    • Displacements were not propagated through the core of the single-domain insulin molecule.
    • Significantly displaced atomic groups were repacked into new conformations, not rigid units.

    Conclusions:

    • Crystal contacts induce localized structural changes in insulin, primarily through atomic repacking.
    • Unlike multi-domain proteins like T4 lysozyme, insulin's single domain limits propagation of large-scale structural changes.
    • Short-range interactions govern the transmission of displacements in insulin, similar to thermal vibrations.