Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Under physiological conditions, a protein undergoes a spontaneous disorder⇌ order
transition called “folding.” The protein polymer is highly flexible when unfolded but adopts its …

A protein backbone structure is designable if a substantial number of amino acid sequences
exist that autonomously fold into it,. It has been suggested that the designability of …

This study views each protein structure as a network of noncovalent connections between
amino acid side chains. Each amino acid in a protein structure is a node, and the strength of …

We propose a novel metaheuristic search for global optimization inspired by the behavior of
a monkey climbing trees looking for food. The tree branches are represented as …

Intrinsically disordered proteins (IDPs) are characterized by substantial conformational
plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to …

As was noted in our recent review, 1 the protein folding field underwent a cyclic
development. Initially, protein folding was viewed as a strictly experimental field belonging to …

Protein aggregation involves the self-assembly of normally soluble proteins into large
supramolecular assemblies. The typical end product of aggregation is the amyloid fibril, an …

Coiled coils are protein structure domains with two or more α-helices packed together via
interlacing of side chains known as knob-into-hole packing. We analysed and classified a …

The shape and size of self‐assembled structures upon local organization of their molecular
building blocks are hard to predict in the presence of long‐range interactions. Combining …