Macromolecular Crowding Facilitates the Conformational Transition of on-Pathway Molten Globule States of the Prion Protein

Fernando Bergasa-Caceres, Herschel Albert Rabitz

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

A simple analytical model is applied to study the effects of macromolecular crowding on the stability of partially folded states of the murine prion protein. It is found that relatively low levels of macromolecular crowding stabilize the partially folded states. The magnitude of the stabilization effect is similar for the partially folded to that of the fully folded state. Thus, the model suggests that it is on-pathway molten globule-like states, rather than partially folded states arising from unfolding of the native state, that play a key role in the pathogenic interconversion mechanism under crowded conditions.

Original languageEnglish (US)
Pages (from-to)11093-11101
Number of pages9
JournalJournal of Physical Chemistry B
Volume120
Issue number43
DOIs
StatePublished - Nov 3 2016

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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