Cargando…
Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins
Intrinsically disordered proteins rich in cationic amino acid groups can undergo Liquid-Liquid Phase Separation (LLPS) in the presence of charge-balancing anionic counterparts. Arginine and Lysine are the two most prevalent cationic amino acids in proteins that undergo LLPS, with arginine-rich prote...
Autores principales: | Hong, Yuri, Najafi, Saeed, Casey, Thomas, Shea, Joan-Emma, Han, Song-I, Hwang, Dong Soo |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9705477/ https://www.ncbi.nlm.nih.gov/pubmed/36443315 http://dx.doi.org/10.1038/s41467-022-35001-1 |
Ejemplares similares
-
Dehydration entropy drives liquid-liquid phase separation by molecular crowding
por: Park, Sohee, et al.
Publicado: (2020) -
Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation
por: Lenard, Aneta J., et al.
Publicado: (2021) -
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
por: Krainer, Georg, et al.
Publicado: (2021) -
The proline-rich domain promotes Tau liquid–liquid phase separation in cells
por: Zhang, Xuemei, et al.
Publicado: (2020) -
Impact of Arginine–Phosphate Interactions on
the Reentrant Condensation of Disordered Proteins
por: Lenton, Samuel, et al.
Publicado: (2021)