Despite advances in machine learning-based protein structure prediction, we are still far
from fully understanding how proteins fold into their native conformation. The conventional …

Computational simulations of protein folding can be used to interpret experimental folding
results, to design new folding experiments, and to test the effects of mutations and small …

Across the Tree of Life (ToL), the complexity of proteomes varies widely. Our systematic
analysis depicts that from the simplest archaea to mammals, the total number of proteins per …

Some misfolded protein conformations can bypass proteostasis machinery and remain
soluble in vivo. This is an unexpected observation, as cellular quality control mechanisms …

The aggregation of medin forming aortic medial amyloid is linked to arterial wall
degeneration and cerebrovascular dysfunction. Elevated levels of arteriolar medin are …

Protein folding and unfolding experiments are interpreted under the assumption of
microscopic reversibility, that is, that at equilibrium one process is the reverse of the other …

Although cooperativity is a well-established and general property of folding, our current
understanding of this feature in multidomain folding is still relatively limited. In fact, there are …

PDZ domains are the most diffused protein–protein interaction modules of the human
proteome and are often present in tandem repeats. An example is PDZD2, a protein …

Subpopulations of soluble, misfolded proteins can bypass chaperones within cells. The
extent of this phenomenon and how it happens at the molecular level are unknown. Through …

Although more than 75% of the proteome is composed of multidomain proteins, current
knowledge of protein folding is based primarily on studies of isolated domains. In this work …