The chaperonins are ubiquitous and essential nanomachines that assist in protein folding in
an ATP-driven manner. They consist of two back-to-back stacked oligomeric rings with …

Protein aggregation propensity is a pervasive and seemingly inescapable property of
proteomes. Strikingly, a significant fraction of the proteome is supersaturated, meaning that …

Many chaperones favour binding to hydrophobic sequences that are flanked by basic
residues while disfavouring acidic residues. However, the origin of this bias in protein quality …

Aggregation can be selectively induced by aggregation-prone regions (APRs) contained in
the target proteins. Aggregation-inducing antimicrobial peptides (Pept-ins) contain …

Cells have evolved a complex molecular network, collectively called the protein
homeostasis (proteostasis) network, to produce and maintain proteins in the appropriate …

Extreme acidophilic bacteria like Leptospirillum sp. require an efficient enzyme system to
counteract strong oxygen stress conditions in their natural habitat. The genome of …

Motivation In vivo protein folding is governed by molecular chaperones, that escort proteins
from their translational birth to their proteolytic degradation. In E. coli the main classes of …

The maintenance of protein homeostasis, also referred to as proteostasis, is essential for
preserving the structural and functional stability of the proteome in living organisms. This …

Development of modern medicine, diagnostics and therapeutics, vaccination programs and
the improvement of living standards have led to the control and even elimination of many …