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PROTEINS: Structure, Function, and Genetics 42:177–181 (2001) StabilizingC-TerminalTailsonAraC MadhushreeGhoshandRobertF.Schleif *

By Abstract Weexaminedtheeffectsofthemetabolic

Abstract

stability of random sequences appended to the C-terminus of the dimerization domain of the regulatoryproteinoftheEscherichiacoliarabinose operon, AraC. Genetic scoring utilized the trans dominant negative effect of the dimerization domain on the activity of intact AraC, and physical scoring used sodium dodecyl sulfate (SDS) gel electrophoresis. We confirmed previous results obtained with Arc and lambda repressors that C-terminalchargedresiduestendtobestabilizingand that hydrophobic residues are destabilizing. Additionally, we found that the provision of a single, charged C-terminal residue conferred significant stabilitythatwasindependentofinteriorsequence. Hence, it appears that in the engineering of proteins, flexible tails may be freely added, with only the identity of the C-terminal amino acid being restricted.Proteins2001;42:177–181. ©2000Wiley-Liss,Inc. Key words: protein stability; AraC; complementatio

Year: 2014
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