Both acute proteotoxic stresses that unfold proteins and expression of disease-causing
mutant proteins that expose aggregation-prone regions can promote protein aggregation …

Protein semisynthesis—defined herein as the assembly of a protein from a combination of
synthetic and recombinant fragments—is a burgeoning field of chemical biology that has …

A major goal in structural biology is to unravel how molecular machines function in detail. To
that end, solution-state NMR spectroscopy is ideally suited as it is able to study biological …

Nuclear import receptors (NIRs) not only transport RNA-binding proteins (RBPs) but also
modify phase transitions of RBPs by recognizing nuclear localization signals (NLSs). Toxic …

Abstract Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases
that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ …

Refolding aggregated proteins is essential in combating cellular proteotoxic stress. Together
with Hsp70, Hsp100 chaperones, including Escherichia coli ClpB, form a powerful …

The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is
expressed throughout the human body. Here, we describe redox-induced changes to the …

The advancements in biotechnology over time have led to an increase in the demand of
pure, soluble and functionally active proteins. Recombinant protein production has thus …

Recent breakthroughs in isotope-labeling and pulse sequence techniques have enabled the
NMR characterization of large protein systems with molecular masses of hundreds of …

Since the release of AlphaFold, researchers have actively refined its predictions and
attempted to integrate it into existing pipelines for determining protein structures. These …