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 Two of these mutations are in helix 3, where Gly-46 and Gly-48 have been replaced by alanines [Hecht, M. H., et al.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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Stearman RS,Frankel AD,Freire E,Liu BS,Pabo COdoi
10.1021/bi00419a059subject
Has Abstractpub_date
1988-09-20 00:00:00pages
7571-4issue
19eissn
0006-2960issn
1520-4995journal_volume
27pub_type
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