Structural preferences shape the entropic force of disordered protein ensembles

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Intrinsically disordered protein regions (IDRs) make up over 30% of the human proteome and instead of a native, well-folded structure exist in a dynamic conformational ensemble. Tethering IDRs to a surface (for example, the surface of a well-folded region of the same protein) can reduce the number o...

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Detalles Bibliográficos
Autores principales: Yu, Feng, Sukenik, Shahar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9882287/
https://www.ncbi.nlm.nih.gov/pubmed/36711874
http://dx.doi.org/10.1101/2023.01.20.524980

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9882287/
https://www.ncbi.nlm.nih.gov/pubmed/36711874
http://dx.doi.org/10.1101/2023.01.20.524980

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