Thermostable protein-stabilized gold nanoclusters as a peroxidase mimic.

Protein-stabilized gold nanoclusters (AuNCs) are fascinating nanostructures with exciting properties owing to their ultra-small sizes and functional shell. However, their applications under extreme conditions are still complicated, waiting for programmable solutions. Therefore, the design of a multi-functional protein stabilizer for specific purposes gains attention to improve the stability and functionality of AuNCs.

Chemical Proteomics of the Tumor Suppressor Fhit Covalently Bound to the Cofactor ApA Elucidates Its Inhibitory Action on Translation.

The tumor suppressor protein (Fhit) is known to be associated with genomic instability and apoptosis. The tumor-suppressive function of Fhit depends on the interaction with the alarmone diadenosine triphosphate (ApA), a noncanonical nucleotide whose concentration increases upon cellular stress. How the Fhit-ApA complex exerts its signaling function is unknown.

Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy.

As one of the most prevalent post-translational modifications in eukaryotic cells, ubiquitylation plays vital roles in many cellular processes, such as protein degradation, DNA metabolism, and cell differentiation. Substrate proteins can be tagged by distinct types of polymeric ubiquitin (Ub) chains, which determine the eventual fate of the modified protein. A facile, click chemistry based approach for the efficient generation of linkage-defined Ub chains, including Ub dimers, was recently established.