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Compaction Properties of an Intrinsically Disordered Protein: Sic1 and Its Kinase-Inhibitor Domain

IDPs in their unbound state can transiently acquire secondary and tertiary structure. Describing such intrinsic structure is important to understand the transition between free and bound state, leading to supramolecular complexes with physiological interactors. IDP structure is highly dynamic and, t...

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Autores principales: Brocca, Stefania, Testa, Lorenzo, Sobott, Frank, Šamalikova, Maria, Natalello, Antonino, Papaleo, Elena, Lotti, Marina, De Gioia, Luca, Doglia, Silvia Maria, Alberghina, Lilia, Grandori, Rita
Formato: Artigo
Lenguaje:Inglês
Publicado: The Biophysical Society 2011
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC3149264/
https://ncbi.nlm.nih.gov/pubmed/21539793
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2011.02.055
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