Cargando…
Controlling Structure and Dimensions of a Disordered Protein via Mutations
The dimensions of intrinsically disordered proteins (IDPs) are sensitive to small energetic-entropic differences between intramolecular and protein–solvent interactions. This is commonly observed on modulating solvent composition and temperature. However, the inherently heterogeneous conformational...
Autores principales: | Munshi, Sneha, Rajendran, Divya, Ramesh, Samyuktha, Subramanian, Sandhyaa, Bhattacharjee, Kabita, Kumar, Meagha Ramana, Naganathan, Athi N. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7115935/ https://www.ncbi.nlm.nih.gov/pubmed/31557007 http://dx.doi.org/10.1021/acs.biochem.9b00678 |
Ejemplares similares
-
Protein plasticity driven by disorder and collapse governs the heterogeneous binding of CytR to DNA
por: Munshi, Sneha, et al.
Publicado: (2018) -
Entropic Control of an Excited Folded-Like Conformation in a Disordered Protein Ensemble
por: Munshi, Sneha, et al.
Publicado: (2018) -
Tunable order–disorder continuum in protein–DNA interactions
por: Munshi, Sneha, et al.
Publicado: (2018) -
Functional regulation of an intrinsically disordered protein via a conformationally excited state
por: Madhurima, Kulkarni, et al.
Publicado: (2023) -
Slow Folding of a Helical Protein: Large Barriers,
Strong Internal Friction, or a Shallow, Bumpy Landscape?
por: Subramanian, Sandhyaa, et al.
Publicado: (2020)