The Physical Driving Forces of Conformational Transition for TTR with Proline Mutations.

Pathological aggregation of essentially dissociated Transthyretin (TTR) monomer proteins, driven by misfolding and self-interaction, is associated with Transthyretin amyloidosis (ATTR) disease. The TTR monomer proteins consist of several fragments that tend to self-aggregate. Recent experimental studies showed that the sequence of residues TTR plays an important role in self-aggregation.

Energy gap of conformational transition related with temperature for the NACore of α-synuclein.

Pathological aggregation of α-synuclein (α-syn) into amyloid fibrils is a major feature of Parkinson's disease (PD). The self-assembly of α-syn is mainly governed by a non-amyloid-β component core (NACore). However, the effects of concentrations and temperatures on their conformational transition remain unclear.