Highlights•Domain swapping refers to the exchange of structural elements between protein
domains.•Experiments show that tandem homologous domains are prone to domain …

Mechanisms of emergence and divergence of protein folds pose central questions in
biological sciences. Incremental mutation and stepwise adaptation explain relationships …

Most foldable protein sequences adopt only a single native fold. Recent protein design
studies have, however, created protein sequences which fold into different structures apon …

Changes at the cell surface enable bacteria to survive in dynamic environments, such as
diverse niches of the human host. Here, we reveal “Periscope Proteins” as a widespread …

Chaperones are a large family of proteins crucial for maintaining cellular protein
homeostasis. One such chaperone is the 70 kDa heat shock protein (Hsp70), which plays a …

Proteins undergo large structural rearrangements such as circular permutations,
dimerisation via domain swapping, and loss of core secondary structure elements in domain …

Abstract Domains are functional and evolutionary units of proteins that typically fold into
stable globular structures. A small subset of natural multidomain proteins contain large …

Proteins are molecules found in all living kingdoms due to their several cellular functions.
They are comprised of amino acids, which are linked together forming long polypeptide …