Heat shock proteins (HSPs) constitute a large family of proteins involved in protein folding
and maturation whose expression is induced by heat shock or other stressors. The major …

Heat shock proteins (HSPs) are a large family of chaperones that are involved in protein
folding and maturation of a variety of “client” proteins protecting them from degradation …

The term “Glomalin” was originally used to describe a hypothetical gene product of
arbuscular mycorrhizal fungi (AMF) that was assumed to be a nearly ubiquitous …

The single gene, single protein, single function hypothesis is increasingly becoming
obsolete. Numerous studies have demonstrated that individual proteins can moonlight …

Structural modeling of macromolecular complexes greatly benefits from interactive
visualization capabilities. Here we present the integration of several modeling tools into …

Efficient folding of many newly synthesized proteins depends on assistance from molecular
chaperones, which serve to prevent protein misfolding and aggregation in the crowded …

▪ Abstract In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the
ubiquitin-proteasome pathway. The 26S proteasome is a 2.5-MDa molecular machine built …

▪ Abstract Uncultured microorganisms comprise the majority of the planet's biological
diversity. Microorganisms represent two of the three domains of life and contain vast …

▪ Abstract Recent years have witnessed dramatic advances in our understanding of how
newly translated proteins fold in the cell and the contribution of molecular chaperones to this …

▪ Abstract In just a few short years, the chemical ligation of unprotected peptide segments in
aqueous solution has established itself as the most practical method for the total synthesis of …