In vivo association of protein fragments giving active AraC

Reconstitution of a native‐like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR

“…Certain single‐domain proteins show native‐like structure and function as noncovalent complexes of their constituent peptide fragments. This complementation of domain fragments has been used to study protein–protein interactions in folding/binding events (Eustance and Schleif 1996; Neira et al 1996; Pecorari et al 1996; Vainshtein et al 1996; Chaffotte et al 1997; Gegg et al 1997; Rietveld and Ferreira 1998; Chakshusmathi et al 1999; Georgescu et al 1999; Goldberg and Baldwin 1999; Honda et al 1999; Kobayashi et al 1999; Tsuji et al 1999; Jourdan and Searle 2000; Yu et al 2000; for review, see de Prat‐Gay 1996) as a method to screen for protein interactions in vivo (Johnsson and Varshavsky 1994; Rossi et al 1997; Pelletier et al 1998; Remy and Michnick 1999) and for developing semisynthetic techniques by religation of the fragments (Homandberg and Laskowski 1979; Vogel and Chmielewski 1994; Vogel et al 1996; for review, see Wallace 1995). Residual structure within the individual peptides of these noncovalent complexes has been investigated as a model for initiation sites of protein folding (Oas and Kim 1988; Wright et al 1988; Dyson et al 1992a, 1992b; for review, see de Prat‐Gay 1996).…”