title: Macromolecular crowding tunes folding landscape of parallel α/β protein, apoflavodoxin.
abstract: Proteins normally fold in crowded cellular environments. Here we use a set of Desulfovibrio desulfuricans apoflavodoxin variants to assess--with residue-specific resolution--how apoflavodoxin's folding landscape is tuned by macromolecular crowding. We find that, under crowded conditions, initial topological frustration is reduced, subsequent folding requires less ordering in the transition state, and β-strand 1 becomes more important in guiding the process. We propose that conditions more closely mimicking the cellular environment make the ensemble of unfolded conformations less expanded, resulting in a folding funnel that is smoother and narrower.
authors.affiliation: Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005, United States.
authors.forename: Loren
authors.initials: L
authors.lastname: Stagg
authors.forename: Alexander
authors.initials: A
authors.lastname: Christiansen
authors.forename: Pernilla
authors.initials: P
authors.lastname: Wittung-Stafshede
mesh_terms: D001059:Apoproteins / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D045285:Desulfovibrio desulfuricans / Q000166:cytology; D005418:Flavodoxin / Q000737:chemistry*; D046911:Macromolecular Substances / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D001059:Apoproteins; D001426:Bacterial Proteins; D005418:Flavodoxin; D046911:Macromolecular Substances; C026932:apoflavodoxin