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Sliding Mechanism at a Coiled-Coil Interface.

David Gomez1, Yulian Gavrilov1, Yaakov Levy1

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Summary
This summary is machine-generated.

Protein coiled coils (CCs) can slide at their interfaces. This study reveals that interface properties influence sliding dynamics, suggesting it

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Area of Science:

  • Protein Science
  • Biophysics
  • Computational Biology

Background:

  • The alpha-helical coiled coil (CC) is a prevalent protein motif.
  • Understanding CC structure-function relationships and dynamics is crucial for protein design.
  • Spontaneous sliding at CC interfaces is observed but mechanistically unclear.

Purpose of the Study:

  • Investigate the mechanism and implications of sliding dynamics at CC interfaces.
  • Determine factors influencing CC interface sliding.
  • Clarify the role of sliding as an intrinsic conformational change in protein-protein interactions.

Main Methods:

  • Utilized coarse-grained and atomistic simulations.
  • Studied various homodimeric CC sequences in parallel and antiparallel configurations.
  • Analyzed the impact of hydrophobic core strength and peripheral salt bridges on sliding.

Main Results:

  • Both hydrophobic core strength and salt bridges significantly affect CC interface sliding dynamics.
  • Energy landscapes for sliding differ between parallel and antiparallel CCs.
  • Free energy barriers for sliding are 1-1.5 kcal/mol, indicating slow kinetics but potential functional relevance.

Conclusions:

  • Sliding at CC interfaces is an intrinsic feature, influenced by interface properties.
  • The findings explain experimentally observed sliding in systems like the dynein stalk.
  • This 1D motion can be a conserved functional mechanism across various CC systems.