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- W2149647521 abstract "Proteins consisting of repeating amino acid motifs are abundant in all kingdoms of life, especially in higher eukaryotes. Repeat-containing proteins self-organize into elongated non-globular structures. Do the same general underlying principles that dictate the folding of globular domains apply also to these extended topologies? Using a simplified structure-based model capturing a perfectly funneled energy landscape, we surveyed the predicted mechanism of folding for ankyrin repeat containing proteins. The ankyrin family is one of the most extensively studied classes of non-globular folds. The model based only on native contacts reproduces most of the experimental observations on the folding of these proteins, including a folding mechanism that is reminiscent of a nucleation propagation growth. The confluence of simulation and experimental results suggests that the folding of non-globular proteins is accurately described by a funneled energy landscape, in which topology plays a determinant role in the folding mechanism." @default.
- W2149647521 created "2016-06-24" @default.
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- W2149647521 date "2005-12-01" @default.
- W2149647521 modified "2023-10-18" @default.
- W2149647521 title "The Energy Landscape of Modular Repeat Proteins: Topology Determines Folding Mechanism in the Ankyrin Family" @default.
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- W2149647521 doi "https://doi.org/10.1016/j.jmb.2005.09.078" @default.
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