Protein aggregation is the main hallmark of neurodegenerative diseases. Many proteins
found in pathological inclusions are known to undergo liquid-liquid phase separation, a …

Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

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 …

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

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 …

We investigate the use of confidence scores to evaluate the accuracy of a given AlphaFold
(AF2) protein model for drug discovery. Prediction of accuracy is improved by not …

This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …

Intrinsically disordered proteins and intrinsically disordered protein regions are highly
abundant in nature. However, the quantitative and qualitative measures of protein intrinsic …

The abundant existence of proteins and regions that possess specific functions without
being uniquely folded into unique 3D structures has become accepted by a significant …