Low-resolution description of the conformational space for intrinsically disordered proteins - Archive ouverte HAL Access content directly
Journal Articles Scientific Reports Year : 2022

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

Abstract

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 and 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, inPress, ⟨10.1038/s41598-022-21648-9⟩. ⟨hal-03796134⟩
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