Alternate Pathways for Folding in the Flavodoxin Fold Family Revealed by a Nucleation-growth Model

Erik D. Nelson, Nick V. Grishin

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

A recent study of experimental results for flavodoxin-like folds suggests that proteins from this family may exhibit a similar, signature pattern of folding intermediates. We study the folding landscapes of three proteins from the flavodoxin family (CheY, apoflavodoxin, and cutinase) using a simple nucleation and growth model that accurately describes both experimental and simulation results for the transition state structure, and the structure of on-pathway and misfolded intermediates for CheY. Although the landscape features of these proteins agree in basic ways with the results of the study, the simulations exhibit a range of folding behaviours consistent with two alternate folding routes corresponding to nucleation and growth from either side of the central β-strand.

Original languageEnglish (US)
Pages (from-to)646-653
Number of pages8
JournalJournal of Molecular Biology
Volume358
Issue number3
DOIs
StatePublished - May 5 2006

Keywords

  • equilibrium intermediates
  • fold families
  • non-native interactions

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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