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• W2029137764 abstract "Protein folding is commonly pictured as a slide down the slopes of a free-energy landscape or 'folding funnel'. Theory predicts that the roughness of such slopes — resulting from local energy traps — should slow folding. Wensley et al. confirm this prediction by demonstrating that the internal friction of preformed helices does cause some members of the 'spectrin' domain family to fold (or unfold) 3,000 times more slowly than others. The authors propose that this unusual feature might have evolved to make spectrins last longer without turnover in red blood cells. The primary sequence of a protein defines its free-energy landscape and thus determines the rate constants of folding and unfolding, with theory suggesting that roughness in the energy landscape leads to slower folding. However, obtaining experimental descriptions of this landscape is challenging. Landscape roughness is now shown to be responsible for the slower folding and unfolding times observed in the R16 and R17 domains of α-spectrin relative to the similar R15 domain. Energy landscape theory is a powerful tool for understanding the structure and dynamics of complex molecular systems, in particular biological macromolecules1. The primary sequence of a protein defines its free-energy landscape and thus determines the folding pathway and the rate constants of folding and unfolding, as well as the protein’s native structure. Theory has shown that roughness in the energy landscape will lead to slower folding1, but derivation of detailed experimental descriptions of this landscape is challenging. Simple folding models2,3 show that folding is significantly influenced by chain entropy; proteins in which the contacts are local fold quickly, owing to the low entropy cost of forming stabilizing, native contacts during folding4,5. For some protein families, stability is also a determinant of folding rate constants6. Where these simple metrics fail to predict folding behaviour, it is probable that there are features in the energy landscape that are unusual. Such general observations cannot explain the folding behaviour of the R15, R16 and R17 domains of α-spectrin. R15 folds ∼3,000 times faster than its homologues, although they have similar structures, stabilities and, as far as can be determined, transition-state stabilities7,8,9,10. Here we show that landscape roughness (internal friction) is responsible for the slower folding and unfolding of R16 and R17. We use chimaeric domains to demonstrate that this internal friction is a property of the core, and suggest that frustration in the landscape of the slow-folding spectrin domains may be due to misdocking of the long helices during folding. Theoretical studies have suggested that rugged landscapes will result in slower folding; here we show experimentally that such a phenomenon directly influences the folding kinetics of a ‘normal’ protein, that is, one with a significant energy barrier that folds on a relatively slow, millisecond–second, timescale." @default.
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• W2029137764 date "2010-02-01" @default.
• W2029137764 modified "2023-10-13" @default.
• W2029137764 title "Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family" @default.
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• W2029137764 doi "https://doi.org/10.1038/nature08743" @default.
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