Flexibility damps macromolecular crowding effects on protein folding dynamics: Application to the murine prion protein (121-231)

Fernando Bergasa-Caceres, Herschel A. Rabitz

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

A model of protein folding kinetics is applied to study the combined effects of protein flexibility and macromolecular crowding on protein folding rate and stability. It is found that the increase in stability and folding rate promoted by macromolecular crowding is damped for proteins with highly flexible native structures. The model is applied to the folding dynamics of the murine prion protein (121-231). It is found that the high flexibility of the native isoform of the murine prion protein (121-231) reduces the effects of macromolecular crowding on its folding dynamics. The relevance of these findings for the pathogenic mechanism are discussed.

Original languageEnglish (US)
Pages (from-to)207-211
Number of pages5
JournalChemical Physics Letters
Volume591
DOIs
StatePublished - Jan 20 2014

All Science Journal Classification (ASJC) codes

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

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