Alternate pathways for folding in the flavodoxin fold family revealed by a nucleation-growth model

J Mol Biol. 2006 May 5;358(3):646-53. doi: 10.1016/j.jmb.2006.02.026. Epub 2006 Mar 3.


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 beta-strand.

MeSH terms

  • Apoproteins / chemistry
  • Apoproteins / metabolism
  • Flavodoxin / chemistry*
  • Flavodoxin / classification
  • Flavodoxin / metabolism*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / classification
  • Membrane Proteins / metabolism*
  • Models, Biological*
  • Models, Molecular
  • Protein Folding*
  • Protein Structure, Tertiary


  • Apoproteins
  • Flavodoxin
  • Membrane Proteins