Protein folding and binding in confined spaces and in crowded solutions

  • Zhou H
  • 81

    Readers

    Mendeley users who have this article in their library.
  • 130

    Citations

    Citations of this article.

Abstract

Simple theoretical models are presented to illustrate the effects of spatial confinement and macromolecular crowding on the equilibria and rates of protein folding and binding. Confinement is expected to significantly stabilize the folded state, but for crowding only a marginal effect on protein stability is expected. In confinement the unfolded chain is restricted to a cage but in crowding the unfolded chain may explore different interstitial voids. Because confinement and crowding eliminate the more expanded conformations of the unfolded state, folding from the compact unfolded state is expected to speed up. Crowding will shift the binding equilibrium of proteins toward the bound state. The significant slowing down in protein diffusion by crowding, perhaps beneficial for chaperonin action, could result in a decrease in protein binding rates.

Author-supplied keywords

  • Chaperonin action
  • Excluded-volume effect
  • Macromolecular crowding
  • Protein aggregation
  • Protein binding
  • Protein folding
  • Spatial confinement

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

  • Huan Xiang Zhou

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free