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  • Title: Combining thermostable mutations increases the stability of lambda repressor.
    Author: Stearman RS, Frankel AD, Freire E, Liu BS, Pabo CO.
    Journal: Biochemistry; 1988 Sep 20; 27(19):7571-4. PubMed ID: 3061460.
    Abstract:
    We have combined three mutations previously shown to stabilize lambda repressor against thermal denaturation. Two of these mutations are in helix 3, where Gly-46 and Gly-48 have been replaced by alanines [Hecht, M. H., et al. (1986) Proteins: Struct., Funct., Genet. 1, 43-46]. The other mutation, which replaces Tyr-88 with cysteine, allows the protein to form an intersubunit disulfide bond [Sauer, R. T., et al. (1986) Biochemistry 25, 5992-5998]. Calorimetric measurements show that the two alanine substitutions stabilize repressor by about 8 degrees C, that the disulfide bond stabilizes repressor by about 8 degrees C, and that the triple mutant is 16 degrees C more stable than wild-type repressor.
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