The phenomena of protein reconstitution and three‐dimensional domain swapping reveal
that highly similar structures can be obtained whether a protein is comprised of one or more …

The native structures of proteins are governed by a large number of non-covalent
interactions yielding a high specificity for the native packing of structural elements. This …

Three-dimensional domain swapping is the process by which two identical protein chains
exchange a part of their structure to form an intertwined dimer or higher-order oligomer. The …

Point mutations in proteins can have different effects on protein stability depending on the
mechanism of unfolding. In the most interesting case of I27, the Ig‐like module of the muscle …

In 3D domain swapping, first described by Eisenberg, a structural element of a monomeric
protein is replaced by the same element from another subunit. This process requires partial …

In the past, many intensive attempts failed to capture or underestimated the copopulated
intermediate conformers from the protein folding/unfolding reaction. We report a promising …

Publisher Summary This chapter examines one type of interchain, noncovalent protein-
protein bond: 3D domain swapping. To date, 3D domain swapping has been definitively …

Three-dimensional domain swapping is the event by which a monomer exchanges part of its
structure with identical monomers to form an oligomer where each subunit has a similar …

A globular protein adopts its native three-dimensional structure spontaneously under
physiological conditions. This structure is specified by a stereochemical code embedded …

The fundamental process by which the amino acid sequence of a protein determines its
native three-dimensional structure is being taken up by an increasing number of …