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Nanomechanics of functional and pathological amyloid materials
Amyloid or amyloid-like fibrils represent a general class of nanomaterials that can be formed
from many different peptides and proteins. Although these structures have an important role …
from many different peptides and proteins. Although these structures have an important role …
Islet amyloid polypeptide: structure, function, and pathophysiology
The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose
homeostasis but aggregates to form islet amyloid in type‐2 diabetes. Islet amyloid formation …
homeostasis but aggregates to form islet amyloid in type‐2 diabetes. Islet amyloid formation …
Molecular mechanism of thioflavin-T binding to the surface of β-rich peptide self-assemblies
A number of small organic molecules have been developed that bind to amyloid fibrils, a
subset of which also inhibit fibrillization. Among these, the benzothiol dye Thioflavin-T (ThT) …
subset of which also inhibit fibrillization. Among these, the benzothiol dye Thioflavin-T (ThT) …
Are current atomistic force fields accurate enough to study proteins in crowded environments?
The high concentration of macromolecules in the crowded cellular interior influences
different thermodynamic and kinetic properties of proteins, including their structural …
different thermodynamic and kinetic properties of proteins, including their structural …
Simulations as analytical tools to understand protein aggregation and predict amyloid conformation
Computational tools are increasingly being applied to solve the protein aggregation
problem, providing insight into amyloid structures and aggregation mechanisms. The …
problem, providing insight into amyloid structures and aggregation mechanisms. The …
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS
The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils
called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar …
called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar …
Modeling the Alzheimer Aβ17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities
We investigate Aβ 17-42 protofibril structures in solution using molecular dynamics
simulations. Recently, NMR and computations modeled the Aβ protofibril as a longitudinal …
simulations. Recently, NMR and computations modeled the Aβ protofibril as a longitudinal …
Aggregation in protein-based biotherapeutics: computational studies and tools to identify aggregation-prone regions
Because of their large, complex, and conformationally heterogeneous structures,
biotherapeutics are vulnerable to several physicochemical stresses faced during the various …
biotherapeutics are vulnerable to several physicochemical stresses faced during the various …
Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p
Sup35p is a prion protein found in yeast that contains a prion-forming domain characterized
by a repetitive sequence rich in Gln, Asn, Tyr, and Gly amino acid residues. The peptide …
by a repetitive sequence rich in Gln, Asn, Tyr, and Gly amino acid residues. The peptide …
Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35
A seven amino acid yeast prion sup-35 fragment (GNNQQNY) forms amyloid fibrils. The
availability of its detailed atomic oligomeric structure makes it a good model for studying the …
availability of its detailed atomic oligomeric structure makes it a good model for studying the …