Peptide self-assembly provides an innovative strategy for not only establishing an ideal
research model to understand life phenomena but also for constructing sophisticated …

Protein structural biology came a long way since the determination of the first three-
dimensional structure of myoglobin about six decades ago. Across this period, X-ray …

Formation of biomolecular condensates through liquid-liquid phase separation (LLPS) has
emerged as a pervasive principle in cell biology, allowing compartmentalization and …

The understanding of the complex conformational landscape of amyloid aggregation and its
modulation by relevant physicochemical and cellular factors is a prerequisite for elucidating …

Phase separation has long been observed within aqueous mixtures of two or more different
compounds, such as proteins, salts, polysaccharides and synthetic polymers. A growing …

Biomolecular condensates formed via phase separation of intrinsically disordered
proteins/regions (IDPs/IDRs) and nucleic acids are associated with cell physiology and …

The solvation shell is essential for the folding and function of proteins, but how it contributes
to protein misfolding and aggregation has still to be elucidated. We show that the mobility of …

Intrinsically disordered proteins (IDPs) or natively unfolded proteins do not undergo
autonomous folding into a well-defined 3-D structure and challenge the conventional …

Recent studies indicate more restricted dynamics of water around intrinsically disordered
proteins (IDPs) than structured proteins. We examine here the dynamics of hydrogen bonds …

Peripheral membrane proteins associate reversibly with biological membranes that,
compared to protein binding partners, are structurally labile and devoid of specific binding …