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Related Experiment Videos

Generalized Crick equations for modeling noncanonical coiled coils.

Gerald Offer1, Matthew R Hicks, Derek N Woolfson

  • 1Muscle Contraction Group, Department of Physiology, Medical School, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom. g.w.offer@bristol.ac.uk

Journal of Structural Biology
|June 18, 2002
PubMed
Summary

This study models complex coiled-coil structures by adapting Crick's equations for non-constant pitch. The new model accurately predicts the atomic coordinates of diverse coiled-coil proteins, advancing our understanding of protein architecture.

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Area of Science:

  • Protein structure and dynamics
  • Biophysics
  • Computational biology

Background:

  • Coiled coils are protein structures formed by alpha-helices.
  • Canonical coiled coils follow heptad repeats, but variations exist.
  • Noncanonical motifs like decad and hendecad alter supercoiling handedness.

Purpose of the Study:

  • To develop a model for coiled coils with mixed heptad, decad, and hendecad motifs.
  • To modify Crick's equations for variable pitch in coiled-coil structures.
  • To test the model's accuracy against experimental data.

Main Methods:

  • Adapted Crick's equations for alpha-helical coiled coils with non-constant pitch.
  • Modeled helix bending using a beam analogy with linearly changing tilt angles.

Related Experiment Videos

  • Applied the model to predict structures of known multi-stranded coiled coils.

    • Main Results:

    • The modified equations successfully modeled coiled coils with mixed motifs.
    • The model accurately predicted backbone atom coordinates for GrpE, hemagglutinin, and tetrabrachion.
    • Achieved root mean square deviations of less than 1.1 Å when comparing model to crystal structures.

    Conclusions:

    • The developed modeling approach accurately captures the structural variations in noncanonical coiled coils.
    • This method provides a framework for understanding and predicting the structures of complex coiled-coil proteins.
    • The findings enhance our understanding of protein folding and stability determinants.