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Related Experiment Videos

A protein folding pathway with multiple folding intermediates at atomic resolution.

Hanqiao Feng1, Zheng Zhou, Yawen Bai

  • 1Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Building 37, Room 6114E, Bethesda, MD 20892, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 29, 2005
PubMed
Summary

Researchers determined the high-resolution structure of a protein folding intermediate using advanced NMR. This reveals key insights into protein folding pathways and dynamics.

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Area of Science:

  • Biochemistry and Structural Biology
  • Protein Dynamics and Folding

Background:

  • Understanding protein folding is crucial for deciphering biological function and disease mechanisms.
  • Previous studies have identified distinct folding intermediates of the Rd-apocytochrome b562 protein.

Purpose of the Study:

  • To determine the high-resolution three-dimensional structure of a specific folding intermediate of the Rd-apocytochrome b562 protein.
  • To elucidate the protein folding pathway at atomic resolution by characterizing multiple intermediates.

Main Methods:

  • Native-state hydrogen-exchange-directed protein engineering.
  • Multidimensional nuclear magnetic resonance (NMR) spectroscopy to determine protein structure.

Main Results:

Related Experiment Videos

  • The high-resolution structure of a key folding intermediate was determined with an rms deviation of 1.1 angstroms.
  • This intermediate features an unfolded N-terminal helix and a partially unfolded C-terminal helix.
  • Combined with previously solved structures, a detailed atomic-resolution description of the protein folding pathway is established.

    • Conclusions:

    • Protein folding intermediates exhibit native-like backbone topology but nonnative side-chain interactions.
    • These findings provide critical data for understanding large-scale conformational searching, -value analysis, and computational protein folding simulations.