Cargando…
Reorientational Dynamics of Amyloid-β from NMR Spin Relaxation and Molecular Simulation
[Image: see text] Amyloid-β (Aβ) aggregation is a hallmark of Alzheimer’s disease. As an intrinsically disordered protein, Aβ undergoes extensive dynamics on multiple length and time scales. Access to a comprehensive picture of the reorientational dynamics in Aβ requires therefore the combination of...
Autores principales: | Rezaei-Ghaleh, Nasrollah, Parigi, Giacomo, Zweckstetter, Markus |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2019
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6598774/ https://www.ncbi.nlm.nih.gov/pubmed/31181936 http://dx.doi.org/10.1021/acs.jpclett.9b01050 |
Ejemplares similares
-
Phosphorylation modifies the molecular stability of β-amyloid deposits
por: Rezaei-Ghaleh, Nasrollah, et al.
Publicado: (2016) -
Interaction between Amyloid Beta Peptide and an Aggregation Blocker Peptide Mimicking Islet Amyloid Polypeptide
por: Rezaei-Ghaleh, Nasrollah, et al.
Publicado: (2011) -
Combined High-Pressure and Multiquantum NMR and Molecular
Simulation Propose a Role for N-Terminal Salt Bridges in Amyloid-Beta
por: Vemulapalli, Sahithya Phani Babu, et al.
Publicado: (2021) -
Water Dynamics in Highly Concentrated Salt Solutions: A Multi‐Nuclear NMR Approach
por: Rezaei‐Ghaleh, Nasrollah
Publicado: (2022) -
Structural Plasticity in Human Heterochromatin Protein 1β
por: Munari, Francesca, et al.
Publicado: (2013)