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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