A simple quantitative model of macromolecular crowding effects on protein folding: Application to the murine prion protein(121-231)

Fernando Bergasa-Caceres, Herschel Albert Rabitz

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

A model of protein folding kinetics is applied to study the effects of macromolecular crowding on protein folding rate and stability. Macromolecular crowding is found to promote a decrease of the entropic cost of folding of proteins that produces an increase of both the stability and the folding rate. The acceleration of the folding rate due to macromolecular crowding is shown to be a topology-dependent effect. The model is applied to the folding dynamics of the murine prion protein (121-231). The differential effect of macromolecular crowding as a function of protein topology suffices to make non-native configurations relatively more accessible.

Original languageEnglish (US)
Pages (from-to)112-115
Number of pages4
JournalChemical Physics Letters
Volume574
DOIs
StatePublished - Jun 14 2013

All Science Journal Classification (ASJC) codes

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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