Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

The protein folding problem was apparently solved recently by the advent of a deep learning
method for protein structure prediction called AlphaFold. However, this program is not able …

Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Intrinsically disordered proteins (IDPs) play many biological roles in the human proteome
ranging from vesicular transport, signal transduction to neurodegenerative diseases. The Aβ …

Self-assembly of amyloid-β peptides leads to oligomers, protofibrils, and fibrils that are likely
instigators of neurodegeneration in Alzheimer's disease. We report results of time-resolved …

Intrinsically disordered proteins (IDPs) are now widely recognized as playing critical roles in
a broad range of cellular functions as well as being implicated in diverse diseases. Their …

The early events in the aggregation of the intrinsically disordered peptide, amyloid-β (A β),
involve transitions from the disordered free energy ground state to assembly-competent …

Förster resonance energy transfer (FRET) is a powerful tool for elucidating both structural
and dynamic properties of unfolded or disordered biomolecules, especially in single …

Protein aggregation is associated with an increasing number of human disorders and
premature aging. Moreover, it is a central concern in the manufacturing of recombinant …

Traumatic brain injury (TBI) elevates Abeta (Aβ) peptides in the brain and cerebral spinal
fluid. Aβ peptides are amphipathic molecules that can modulate membrane mechanics …