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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: | , , , , , , , , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
The Biophysical Society
2011
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| Materias: | |
| 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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