Highlights•Single molecule FRET experiments determine average transition path
times.•Observed times are extremely close to those found in all-atom MD simulations.•Times …

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

Protein folding is assisted by molecular chaperones that bind nascent polypeptides during
mRNA translation. Several structurally distinct classes of chaperones promote de novo …

The folding process of multidomain proteins is a highly intricate phenomenon involving the
assembly of distinct domains into a functional three-dimensional structure. During this …

Protein folding and unfolding experiments are interpreted under the assumption of
microscopic reversibility, that is, that at equilibrium one process is the reverse of the other …

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 …

Abstract GRB2, or Growth Factor Receptor-Bound Protein 2, is a pivotal adaptor protein in
intracellular signal transduction pathways, particularly within receptor tyrosine kinase (RTK) …

Although cooperativity is a well-established and general property of folding, our current
understanding of this feature in multidomain folding is still relatively limited. In fact, there are …

Many eukaryotic proteins contain intrinsically disordered regions (IDRs) that intersperse
globular folded domains, in contrast with bacterial proteins which are typically highly …

Although more than 75% of the proteome is composed of multidomain proteins, current
knowledge of protein folding is based primarily on studies of isolated domains. In this work …