Jump to main content
Jump to site search

Volume 106, 2010
Previous Article Next Article

Studies of protein folding pathways

Author affiliations

Abstract

Protein folding is a problem of great importance in both the life sciences and biotechnology industries. This review begins with a brief summary of the physics of protein folding in vivo, which we believe would provide a theoretical basis for the kinetic control of protein folding. This is followed by a summary of the established refolding methods, which are categorized according to their process kinetics. Molecular simulations are used to present the concept of establishing dynamic solution environments that mimic the molecular machinery employed for high efficiency protein folding in vivo to enhance the kinetic partitioning of the native conformation. In practice, the use of “SMARTpolymers for protein folding in a decreasing temperature gradient mimics the capture-release mechanism of GroEL/GroES/ATP and promotes protein folding and inhibits protein aggregation. Oscillation of the oxidative/reductive potential of the solution by periodic loading of redox chemicals promotes the reshuffling of disulfide bridges, mimicking the action of protein disulfide isomerase (PDI), and results in increased refolding yields. Realization of the simulated “oscillatory hydrophobic driving force” that mimics the quality control system in the endoplasmic reticulum (ER) may be of enormous practical value for protein folding at high concentrations.

Back to tab navigation

Publication details

The article was first published on 29 Mar 2010


Article type: Review Article
DOI: 10.1039/B903487K
Annu. Rep. Prog. Chem., Sect. C: Phys. Chem., 2010,106, 259-273

  •   Request permissions

    Studies of protein folding pathways

    D. Lu and Z. Liu, Annu. Rep. Prog. Chem., Sect. C: Phys. Chem., 2010, 106, 259
    DOI: 10.1039/B903487K

Search articles by author

Spotlight

Advertisements