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 …

BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …

The bacterial chaperonin GroEL and its cofactor GroES constitute the paradigmatic
molecular machine of protein folding. GroEL is a large double-ring cylinder with ATPase …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …

Cellular chaperone networks prevent potentially toxic protein aggregation and ensure
proteome integrity. Here, we used Escherichia coli as a model to understand the …

The timely production of functional proteins is of critical importance for the biological activity
of cells. To reach the functional state, newly synthesized polypeptides have to become …

Although the sequence of a protein largely determines its function, proteins can adopt
different folding states in response to changes in the environment, some of which may be …

Proteins are increasingly used in basic and applied biomedical research. Many proteins,
however, are only marginally stable and can be expressed in limited amounts, thus …