Macromolecular Crowding Tunes Folding Landscape of Parallel 伪/尾 Protein, Apoflavodoxin

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• 作者：Loren Stagg ; Alexander Christiansen ; Pernilla Wittung-Stafshede
• 刊名：Journal of the American Chemical Society
• 出版年：2011
• 出版时间：February 2, 2011
• 年：2011
• 卷：133
• 期：4
• 页码：646-648
• 全文大小：671K
• 年卷期：v.133,no.4(February 2, 2011)
• ISSN：1520-5126

文摘

Proteins normally fold in crowded cellular environments. Here we use a set of Desulfovibrio desulfuricans apoflavodoxin variants to assess鈥攚ith residue-specific resolution鈥攈ow apoflavodoxin鈥檚 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 尾-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.