Protein instability caused by exposure to external additives or severe stress may result in
different diseases. Of these diseases, many are triggered by protein misfolding and …

Oligomers which form during amyloid fibril assembly are considered to be key contributors
towards amyloid disease. However, understanding how such intermediates form, their …

Intracellular aggregation of the human amyloid protein α-synuclein is causally linked to
Parkinson's disease. While the isolated protein is intrinsically disordered, its native structure …

Aggregation of human α-synuclein (αSyn) is linked to Parkinson's disease (PD) pathology.
The central region of the αSyn sequence contains the non-amyloid β-component (NAC) …

Alpha-synuclein (αSyn) is a protein involved in neurodegenerative disorders including
Parkinson's disease. Amyloid formation of αSyn can be modulated by the 'P1 …

As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large
conformational space. Certain conformations lead to aggregation prone and non …

Intrinsically disordered proteins (IDPs) are implicated in many human diseases. They have
generally not been amenable to conventional structure-based drug design, however …

There is growing interest in the development of physical methods to study the
conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In …

The aggregation of the intrinsically disordered protein alpha-synuclein (α S) into amyloid
fibrils is thought to play a central role in the pathology of Parkinson's disease. Using a …

Alzheimer's disease (AD) and Parkinson's disease (PD) are age-associated
neurodegenerative disorders characterized by the misfolding and aggregation of alpha …