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Van der Waals locks: loop-n-lock structure of globular proteins.

I N Berezovsky1, E N Trifonov

  • 1Department of Structural Biology, The Weizmann Institute of Science, Rehovot, 76100, Israel. Igor.Berezovwsky@weizmann.ac.il

Journal of Molecular Biology
|April 9, 2001
PubMed
Summary

Globular protein stability is maintained by van der Waals interactions. This study identifies "van der Waals locks" within protein structures, revealing a novel "loop-n-lock" organization crucial for protein folding.

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Area of Science:

  • Protein structure and stability
  • Biophysics
  • Structural biology

Background:

  • Globular proteins feature complex polypeptide chain folding with numerous chain-to-chain contacts.
  • Van der Waals interactions are the primary forces stabilizing these protein structures.

Purpose of the Study:

  • To analyze van der Waals contacts stabilizing the spatial structures of nine major protein folds.
  • To introduce a method for identifying critical van der Waals contacts and the concept of a 'van der Waals lock'.

Main Methods:

  • Isolation and analysis of van der Waals contacts in crystallized proteins.
  • Identification of the tightest contacts crucial for protein stability.

Main Results:

  • A novel structural motif, the 'loop-n-lock' structure, is proposed, where loops are closed by van der Waals interactions.

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  • Specific van der Waals contacts of prime importance for protein stability were identified.

    • Conclusions:

    • The 'loop-n-lock' structure offers a new perspective on protein globule organization.
    • This finding provides new insights into the mechanisms of protein folding, emphasizing the role of sequential looping and locking via van der Waals forces.