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- W242119928 abstract "This chapter discusses protein–protein interaction in the α-complementation system of β-galactosidase. α-complementation system in β-galactosidase system is a system of protein–protein interaction where active enzyme is formed through the association of two different polypeptide chains encoded by different lacZ alleles. The chapter presents some of the key features of α-complementation. β-galactosidase is a tetrameric enzyme. The rate-determining step in α-complementation is the conversion of inactive dimeric proteins, termed α-acceptors, to catalytically active tetramers. The most thoroughly studied α-donor analyzed in vitro is a cyanogen bromide peptide derived from β-galactosidase, comprising amino acid residues 3–92 of the wild-type protein. Either the M15 protein, lacking residues 11–41, or the M112 protein, with a smaller deletion of residues 23–31, are able to serve as α-acceptors. Immunochemical analyses and amino acid sequence comparisons of the α-donor and α-acceptor molecules suggest that residues 23–31 of β-galactosidase play a critical role in the dimerization of M15 dimers." @default.
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- W242119928 date "1992-01-01" @default.
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- W242119928 title "Protein-Protein Interaction in the α-Complementation System of β-Galactosidase" @default.
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- W242119928 doi "https://doi.org/10.1016/b978-0-12-152833-1.50011-3" @default.
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