Macromolecular crowding tunes folding landscape of parallel α/β protein, apoflavodoxin
2011 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 133, no 4, 646-648 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
American Chemical Society (ACS), 2011. Vol. 133, no 4, 646-648 p.
IdentifiersURN: urn:nbn:se:umu:diva-38759DOI: 10.1021/ja107638ePubMedID: 21175168OAI: oai:DiVA.org:umu-38759DiVA: diva2:381554