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Related Experiment Videos

Different folding transition states may result in the same native structure

A R Viguera1, L Serrano, M Wilmanns

  • 1EMBL, Heidelberg, Germany.

Nature Structural Biology
|October 1, 1996
PubMed
Summary
This summary is machine-generated.

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Circularly permuted alpha-spectrin SH3 domains retain wild-type structure but exhibit altered folding transition states. This suggests protein native and transition states are not directly related.

Area of Science:

  • Protein structure and folding
  • Structural biology
  • Biochemistry

Background:

  • Alpha-spectrin SH3 domain is a well-studied protein folding model.
  • Circular permutation can alter protein folding pathways.
  • Understanding protein folding intermediates is crucial for protein stability and function.

Purpose of the Study:

  • Determine the crystal structures of two circular permutants of the alpha-spectrin SH3 domain.
  • Investigate the impact of circular permutation on protein folding.
  • Examine the relationship between native structures and folding transition states.

Main Methods:

  • X-ray crystallography to determine protein structures at high resolution (2.02 Å and 1.77 Å).
  • Analysis of folding kinetics using eight point mutants to study transition states.

Related Experiment Videos

  • Comparison of structural and kinetic data between wild-type and permuted SH3 domains.

    • Main Results:

    • Both circular permutants adopt similar 3D structures to wild-type alpha-spectrin SH3 domain.
    • Cleavage of the RT loop in one permutant leads to hydrogen bond unzipping.
    • Transition states for folding differ significantly among the wild-type and permuted proteins.

    Conclusions:

    • Circular permutation in alpha-spectrin SH3 domain does not disrupt the overall fold.
    • Protein folding transition states can vary independently of the native structure.
    • There is no direct correlation between the native state and the transition state of protein folding.