Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

Protein stability is not just an academic matter. Biotechnology, Cell Biology and Drug Design
are some of the fields where both theoretical and practical knowledge of protein stability is …

ATP-independent chaperones are usually considered to be holdases that rapidly bind to
non-native states of substrate proteins and prevent their aggregation. These chaperones are …

Despite advances in artificial intelligence methods, protein folding remains in many ways an
enigma to be solved. Accurate computation of protein folding energetics could help drive …

We study the behavior of a classical two-component ionic plasma made up of nonadditive
hard disks with additional logarithmic Coulomb interactions between them. Due to the …

Molten globule (MG) is the name given to a compact, non‐native conformation of proteins
that has stimulated the imagination and work in the protein folding field for more than 40 …

Increasing the thermostability of proteins is often crucial for their successful use as analytic,
synthetic or therapeutic tools. Most rational thermostabilization strategies were developed …

Intermediate conformations are crucial to our understanding of how proteins fold into their
native structures and become functional. Conventional spectroscopic measurements of …

The possibility of the protein backbone adopting lasso-like entangled motifs has attracted
increasing attention. After discovering the surprising abundance of natively entangled …

Streptococcus pneumoniae (Sp) strain TIGR4 is a virulent, encapsulated serotype that
causes bacteremia, otitis media, meningitis and pneumonia. Increased bacterial resistance …