The intriguing process of protein folding comprises discrete steps that stabilize the protein
molecules in different conformations. The metastable state of protein is represented by …

Conformational properties of intrinsically disordered proteins (IDPs) are governed by a
sequence-ensemble relationship. To differentiate the impact of sequence-local versus …

We review the current state on the thermodynamic behavior and structural phases of self-
and mutually-attractive dilute semiflexible polymers that undergo temperature-driven …

As a model of self-assembly from disordered monomers to fibrils, the amyloid-β fragment
Aβ16-22 was subject to past numerous experimental and computational studies. Because …

Probing the structures of amyloid‐β (Aβ) peptides in the early steps of aggregation is
extremely difficult experimentally and computationally. Yet, this knowledge is extremely …

Although temperature-dependent self-assembly kinetics is usually described by approaches
which assume that the macromolecular aggregates have a definite shape, sometimes that …

It is well established that amyloid fibril solubility is protein specific, but how solubility
depends on the interactions between the fibril building blocks is not clear. Here we use a …

We focused on the relation between the intrinsic disorder of α-syn and macromolecular
crowding, and constructed a lattice gas model of α-syn including crowding agents based on …

Microcanonical thermostatistics analysis has been introduced as an important method in the
study of phase transitions observed in intrinsically small systems, such as folding transitions …

We draw an analogy between droplet formation in dilute particle and polymer systems. Our
arguments are based on finite-size scaling results from studies of a two-dimensional lattice …