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Cover Illustration: Reconstitution of proteins to native-like folded states from constituent fragments is a reaction common to a large number of proteins with widely varying structures. The ability of even disordered fragments to reassemble indicates that the reconstitution reaction is akin to protein folding. Here, the N- and C-terminal domains of intact calmodulin (green and blue, respectively, with darker and lighter tones distinguishing each EF hand) are shown grasping a target peptide (pink) from myosin light chain kinase (top). The exploded and rotated view (middle) reveals complementary hydrophobic patches (yellow or orange); secondary structures are shown in ribbons below. Assembly of the ternary complex requires the presence of calcium (purple spheres). Reconstitution and the related process of three-dimensional domain swapping have in common the fact that the tertiary structure begins in one polypeptide chain and is completed using segments from another chain. In contrast to ordinary protein-folding reactions, the extent of folding by either reconstitution or domain swapping depends on protein concentration. In the review by Carey et al. (this issue), reconstitution is used as a lens through which to examine the process of protein folding, as well as related protein phenomena including domain swapping, circular permutation, natively unfolded states, and ligand-coupled folding. (See Carey et al. pp. 2317-2333.)