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Pathways of protein folding

C R Matthews1

  • 1Department of Chemistry, Pennsylvania State University, University Park 16802.

Annual Review of Biochemistry
|January 1, 1993
PubMed
Summary
This summary is machine-generated.

Protein folding progresses through three key stages: initial collapse, development of secondary and tertiary structures, and final stabilization. This process involves dynamic equilibria and evolving structural complexity over time.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Physical Chemistry

Background:

  • Advances in spectroscopy, protein engineering, and peptide synthesis have improved understanding of protein folding.
  • Protein folding involves transient intermediates and dynamic structural changes.

Purpose of the Study:

  • To elucidate the common stages and characteristics of protein folding.
  • To describe the kinetic and thermodynamic aspects of protein folding intermediates.

Main Methods:

  • Analysis of data from various proteins using spectroscopy and protein engineering.
  • Characterization of transient folding intermediates and their conformational ensembles.

Main Results:

  • Identified three common stages in protein folding: initial collapse, intermediate structure formation, and final stabilization.

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  • Characterized the thermodynamic stability and conformational dynamics of each folding stage.
  • Described folding as a series of transitions between dynamic structural equilibria rather than a single pathway.

    • Conclusions:

    • Protein folding is a stepwise process with increasing structural order and stability.
    • Each stage involves an ensemble of conformations, with complexity reducing over time.
    • The folding process is better described as transitions between dynamic equilibria than a fixed pathway.