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Related Experiment Videos

Water-inserted alpha-helical segments implicate reverse turns as folding intermediates.

M Sundaralingam1, Y C Sekharudu

  • 1Department of Biochemistry, University of Wisconsin-Madison 53706.

Science (New York, N.Y.)
|June 16, 1989
PubMed
Summary
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Protein alpha helices can fold and unfold via water-inserted intermediates. These intermediates, observed in crystal structures, reveal hydration mechanisms and conformational changes, suggesting a folding pathway in solution.

Area of Science:

  • Structural biology
  • Biochemistry
  • Protein folding

Background:

  • Alpha helices are fundamental protein secondary structures.
  • Understanding protein folding and unfolding is crucial in biochemistry.
  • Hydration plays a significant role in protein structure and dynamics.

Purpose of the Study:

  • To investigate the role of water in the folding and unfolding of alpha helices.
  • To identify potential intermediates in the alpha helix folding pathway.
  • To propose a folding-unfolding pathway for alpha helices in aqueous solution.

Main Methods:

  • Analysis of protein crystal structures.
  • Identification of hydrated alpha-helical segments.
  • Characterization of reverse-turn conformations within these segments.

Related Experiment Videos

  • Conformational analysis of dihedral angles (phi, psi).

    • Main Results:

    • Alpha helices in protein crystal structures are hydrated by water molecules.
    • Water molecules can interact externally or internally with the helix backbone.
    • Water-inserted segments exhibit various reverse-turn conformations (e.g., type III, II, I).
    • These conformations resemble folding intermediates trapped during the folding-unfolding process.

    Conclusions:

    • Water-inserted alpha-helical segments represent key intermediates in protein folding.
    • The observed conformations suggest a plausible pathway for alpha helix folding and unfolding in aqueous solution.
    • The study provides insights into the dynamics of protein secondary structure formation.