Recent years have witnessed major advances in our understanding of the structural basis of
protein aggregation on several fronts. Firstly, high-resolution structural information that …

Nanostructured scaffolds recently showed great promise in tissue engineering:
nanomaterials can be tailored at the molecular level and scaffold morphology may more …

Experimental findings suggest that oligomeric forms of the amyloid β protein (Aβ) play a
critical role in Alzheimer's disease. Thus, elucidating their structure and the mechanisms of …

Since the reformulation of the amyloid cascade hypothesis to focus on oligomeric
aggregates of amyloid beta as the prime toxic species causing Alzheimer's disease, many …

The alpha-helix to beta-sheet transition (α-β transition) is a universal deformation
mechanism in alpha-helix rich protein materials such as wool, hair, hoof, and cellular …

The free energy landscape for folding of the Alzheimer's amyloid-β (25–35) peptide is
explored using replica exchange molecular dynamics in both pure water and in HFIP/water …

Self-assembly at the nanoscale is becoming increasingly important for the fabrication of
novel supramolecular structures, with applications in the fields of nanobiotechnology and …

The aggregation of amyloid beta (Aβ) peptides plays an important role in the development of
Alzheimer's disease. Despite extensive effort, it has been difficult to characterize the …

We characterized the α-to-β transition in α-helical coiled-coil connectors of the human fibrin
(ogen) molecule using biomolecular simulations of their forced elongation and theoretical …

The propensity to form fibril in disease-related proteins is a widely studied phenomenon, but
its correlation, if any, with structural characteristics of the associated proteins is not clearly …