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 Biochemjournal_title
Journal of cellular biochemistryauthors
Hecht MH,Hehir KM,Nelson HC,Sturtevant JM,Sauer RTdoi
10.1002/jcb.240290306subject
Has Abstractpub_date
1985-01-01 00:00:00pages
217-24issue
3eissn
0730-2312issn
1097-4644journal_volume
29pub_type
杂志文章abstract::Survivin is a member of the inhibitor of apoptosis (IAP) gene family, containing a single baculovirus IAP repeat (BIR) and no RING finger, that is expressed in many human cancers. Although it has been proposed to be involved in mitotic and cytokinetic processes, its functional subcellular distribution in the cytoplasm...
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