Cargando…
Enhanced accessibility and hydrophobicity of amyloidogenic intermediates of the β2-microglobulin D76N mutant revealed by high-pressure experiments
β2-Microglobulin (β2m) is the causative protein of dialysis-related amyloidosis. Its unfolding mainly proceeds along the pathway of N(C) →U(C) ⇄ U(T), whereas refolding follows the U(T) → I(T) (→N(T)) →N(C) pathway, in which N, I, and U are the native, intermediate, and unfolded states, respectively...
Autores principales: | Sakurai, Kazumasa, Tomiyama, Ryosuke |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7950326/ https://www.ncbi.nlm.nih.gov/pubmed/33508321 http://dx.doi.org/10.1016/j.jbc.2021.100333 |
Ejemplares similares
-
Loosening of Side-Chain Packing Associated with Perturbations in Peripheral Dynamics Induced by the D76N Mutation of β(2)-Microglobulin Revealed by Pressure-NMR and Molecular Dynamic Simulations
por: Sakurai, Kazumasa, et al.
Publicado: (2019) -
Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin
por: Chong, Song-Ho, et al.
Publicado: (2015) -
The residual structure of acid‐denatured β(2)‐microglobulin is relevant to an ordered fibril morphology
por: Tomiyama, Ryosuke, et al.
Publicado: (2023) -
A Simulated Intermediate State for Folding and Aggregation Provides Insights into ΔN6 β(2)-Microglobulin Amyloidogenic Behavior
por: Estácio, Sílvia G., et al.
Publicado: (2014) -
Decoding the Structural Bases of D76N ß2-Microglobulin High Amyloidogenicity through Crystallography and Asn-Scan Mutagenesis
por: de Rosa, Matteo, et al.
Publicado: (2015)