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Conformational ensembles of the human intrinsically disordered proteome
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“Developments in protein structural prediction have given researchers a transformative ability to predict the structures of folded proteins, and to perform structure-based analyses of protein function at the proteome level 2 .”
InfluentialSelf-citationAlphaFold and Implications for Intrinsically Disordered Proteins
Ruff, K. M., & Pappu, R. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167208 · Cited by 635 · cited 1×
“When methods such as AlphaFold are applied to IDRs, however, they result in a single configuration or few configurations of low confidence, which do not represent the conformational heterogeneity and functional states of IDRs 6 .”
Conformational buffering underlies functional selection in intrinsically disordered protein regions
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- Tesei, G., Trolle, A. I., Jonsson, N., Betz, J., Knudsen, F. E., Pesce, F., Johansson, K. E., & Lindorff-Larsen, K.
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- 1476-4687
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