Title

Protein folding and three-dimensional domain swapping: A strained relationship?

Document Type

Article

Publication Date

2-1-2002

Abstract

Many proteins function as multimeric assemblies into which the folded individual promoters organize as higher order structures. An oligomerization mechanism that appears to impose the coordination of events during folding and oligomer assembly is three-dimensional domain swapping. Recent studies have focused on revealing the structural basis of domain swapping and a possible role for domain swapping in the regulation of protein aggregation and activity.

Publication Source (Journal or Book title)

Current Opinion in Structural Biology

First Page

48

Last Page

53

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