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Article Dans Une Revue Scientific Reports Année : 2022

Low-resolution description of the conformational space for intrinsically disordered proteins

Résumé

Intrinsically disordered proteins (IDP) are at the center of numerous biological processes, and attract consequently extreme interest in structural biology. A systematic enumeration of protein conformations, carried out using the TAiBP approach based on the distance geometry, was performed on two proteins, Sic1 and pSic1, corresponding to unphosphorylated and phosphorylated states of an IDP. The populated conformations
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Dates et versions

hal-03796134 , version 1 (04-10-2022)

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Daniel Förster, Leo Liberti, Antonio Mucherino, Jung-Hsin Lin, Thérèse E Malliavin, et al.. Low-resolution description of the conformational space for intrinsically disordered proteins. Scientific Reports, In press, ⟨10.1038/s41598-022-21648-9⟩. ⟨hal-03796134⟩
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