Cargando…
Diffusion-limited association of disordered protein by non-native electrostatic interactions
Intrinsically disordered proteins (IDPs) usually fold during binding to target proteins. In contrast to interactions between folded proteins, this additional folding step makes the binding process more complex. Understanding the mechanism of coupled binding and folding of IDPs requires analysis of b...
Autores principales: | Kim, Jae-Yeol, Meng, Fanjie, Yoo, Janghyun, Chung, Hoi Sung |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6226484/ https://www.ncbi.nlm.nih.gov/pubmed/30413699 http://dx.doi.org/10.1038/s41467-018-06866-y |
Ejemplares similares
-
Single-molecule fluorescence imaging and deep learning reveal highly heterogeneous aggregation of amyloid-β 42
por: Meng, Fanjie, et al.
Publicado: (2022) -
Fast three-color single-molecule FRET using statistical inference
por: Yoo, Janghyun, et al.
Publicado: (2020) -
Role of non-native electrostatic interactions in the coupled folding and binding of PUMA with Mcl-1
por: Chu, Wen-Ting, et al.
Publicado: (2017) -
Electrostatic Stabilization of a Native Protein Structure in the Gas Phase**
por: Breuker, Kathrin, et al.
Publicado: (2011) -
Interpreting protein/DNA interactions: distinguishing specific from non-specific and electrostatic from non-electrostatic components
por: Privalov, Peter L., et al.
Publicado: (2011)