Many proteins and protein segments cannot attain a single stable three-dimensional
structure under physiological conditions; instead, they adopt multiple interconverting …

Recognition of the natural abundance and functional importance of intrinsically disordered
proteins (IDPs), and protein hybrids that contain both intrinsically disordered protein regions …

Abstract Arginine shows Jekyll and Hyde behavior in several respects. It participates in
protein folding via ionic and H-bonds and cation-pi interactions; the charge and …

Allostery is the process by which biological macromolecules (mostly proteins) transmit the
effect of binding at one site to another, often distal, functional site, allowing for regulation of …

Intrinsically disordered proteins (IDPs) and IDP regions fail to form a stable structure, yet
they exhibit biological activities. Their mobile flexibility and structural instability are encoded …

Proteins are the major component of the living cell. They play crucial roles in the
maintenance of life, and their dysfunctions are known to cause different pathologies. One of …

Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs)
are functional proteins and domains that devoid stable secondary and/or tertiary structure …

The intracellular environment represents an extremely crowded milieu, with a limited amount
of free water and an almost complete lack of unoccupied space. Obviously, slightly salted …

Intrinsically disordered proteins (IDPs) are unable to adopt a unique 3D structure under
physiological conditions and thus exist as highly dynamic conformational ensembles. IDPs …

At the turn of the twenty-first century, fundamental changes took place in the understanding
of the structure and function of proteins and then in the appreciation of the intracellular …