Abstract α-synuclein (αS) is an intrinsically disordered protein whose fibrillar aggregates are
the major constituents of Lewy bodies in Parkinson's disease. Although the specific function …

Abstract α-Synuclein (αS) is a presynaptic disordered protein whose aberrant aggregation is
associated with Parkinson's disease. The functional role of αS is still debated, although it …

The aggregation of α-synuclein (αS), a protein abundant at presynaptic terminals, is
associated with a range of highly debilitating neurodegenerative conditions, including …

The identification of the factors that enable normally folded proteins to remain in their soluble
and functional states is crucial for a comprehensive understanding of any biological system …

α-Synuclein (αS) is a presynaptic protein whose aggregation is associated with Parkinson's
disease (PD). Although the physiological function of αS is still unclear, several lines of …

The aggregation process of peptides and proteins is of great relevance as it is associated
with a wide range of highly debilitating disorders, including Alzheimer's and Parkinson's …

Folding of polypeptide chains into biologically active entities is an astonishingly complex
process, determined by the nature and the sequence of residues emerging from ribosomes …

The characterization of intrinsically disordered regions (IDRs) in membrane-associated
proteins is of crucial importance to elucidate key biochemical processes, including cellular …

Water at the protein surface is an active biological molecule that plays a critical role in many
functional processes. Using NMR-restrained MD simulations, we here addressed how …

Proteins from hyperthermophilic organisms are evolutionary optimised to adopt functional
structures and dynamics under conditions in which their mesophilic homologues are …