Recent force field strategies for intrinsically disordered proteins
Intrinsically disordered proteins (IDPs) are widely distributed across eukaryotic cells, playing
important roles in molecular recognition, molecular assembly, post-translational …
important roles in molecular recognition, molecular assembly, post-translational …
Amyloid aggregation simulations: challenges, advances and perspectives
B Strodel - Current opinion in structural biology, 2021 - Elsevier
In amyloid aggregation diseases soluble proteins coalesce into a wide array of undesirable
structures, ranging through oligomers and prefibrillar assemblies to highly ordered amyloid …
structures, ranging through oligomers and prefibrillar assemblies to highly ordered amyloid …
A hairpin motif in the amyloid-β peptide is important for formation of disease-related oligomers
The amyloid-β (Aβ) peptide is associated with the development of Alzheimer's disease and
is known to form highly neurotoxic prefibrillar oligomeric aggregates, which are difficult to …
is known to form highly neurotoxic prefibrillar oligomeric aggregates, which are difficult to …
AlphaFold2: a role for disordered protein/region prediction?
The development of AlphaFold2 marked a paradigm-shift in the structural biology
community. Herein, we assess the ability of AlphaFold2 to predict disordered regions …
community. Herein, we assess the ability of AlphaFold2 to predict disordered regions …
Aging can transform single-component protein condensates into multiphase architectures
A Garaizar, JR Espinosa, JA Joseph… - Proceedings of the …, 2022 - National Acad Sciences
Phase-separated biomolecular condensates that contain multiple coexisting phases are
widespread in vitro and in cells. Multiphase condensates emerge readily within …
widespread in vitro and in cells. Multiphase condensates emerge readily within …
Disorder-to-order transition of the amyloid-β peptide upon lipid binding
There is mounting evidence that Alzheimer's disease progression and severity are linked to
neuronal membrane damage caused by aggregates of the amyloid-β (A β) peptide …
neuronal membrane damage caused by aggregates of the amyloid-β (A β) peptide …
Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane
Mounting evidence suggests that the neuronal cell membrane is the main site of oligomer-
mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed …
mediated neuronal toxicity of amyloid-β peptides in Alzheimer's disease. To gain a detailed …
Protein structural transitions critically transform the network connectivity and viscoelasticity of RNA-binding protein condensates but RNA can prevent it
AR Tejedor, I Sanchez-Burgos… - Nature …, 2022 - nature.com
Biomolecular condensates, some of which are liquid-like during health, can age over time
becoming gel-like pathological systems. One potential source of loss of liquid-like properties …
becoming gel-like pathological systems. One potential source of loss of liquid-like properties …
[HTML][HTML] Self-assembling peptide biomaterials: Insights from spontaneous and enhanced sampling molecular dynamics simulations
BJ Williams-Noonan, A Kamboukos… - Chemical Physics …, 2023 - pubs.aip.org
Peptide self-assembly is the process by which peptide molecules aggregate into low
dimensional (1D, 2D) or 3D ordered materials with potential applications ranging from drug …
dimensional (1D, 2D) or 3D ordered materials with potential applications ranging from drug …
Insights into the atomistic mechanisms of phosphorylation in disrupting liquid–liquid phase separation and aggregation of the FUS low-complexity domain
Fused in sarcoma (FUS), a nuclear RNA binding protein, can not only undergo liquid–liquid
phase separation (LLPS) to form dynamic biomolecular condensates but also aggregate into …
phase separation (LLPS) to form dynamic biomolecular condensates but also aggregate into …