Increasing and decreasing protein stability: effects of revertant substitutions on the thermal denaturation of phage lambda repressor.

Abstract:

:The thermal denaturations of five revertant lambda repressors containing single amino acid substitutions in their N-terminal domains have been studied by differential scanning calorimetry. Two substitutions slightly decrease stability, and the remaining three render the protein more stable than wild type. The Gly48----Asn and Gly48----Ser proteins are 4 degrees C more stable than wild type. These two substitutions replace an alpha helical residue, and in each case a poor helix forming residue, glycine, is replaced by a residue with a higher helical propensity. We also present data showing that one revertant, Tyr22----Phe, has reduced operator DNA binding affinity despite its enhanced stability.

journal_name

J Cell Biochem

authors

Hecht MH,Hehir KM,Nelson HC,Sturtevant JM,Sauer RT

doi

10.1002/jcb.240290306

subject

Has Abstract

pub_date

1985-01-01 00:00:00

pages

217-24

issue

3

eissn

0730-2312

issn

1097-4644

journal_volume

29

pub_type

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