TY - JOUR
T1 - Increasing and decreasing protein stability
T2 - Effects of revertant substitutions on the thermal denaturation of phage λ repressor
AU - Hecht, Michael H.
AU - Hehir, Kathleen M.
AU - Nelson, Hillary C.M.
AU - Sturtevant, Julian M.
AU - Sauer, Robert T.
PY - 1985
Y1 - 1985
N2 - The thermal denaturations of five revertant λ 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°C more stable than wild type. These two substitutions replace an α 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.
AB - The thermal denaturations of five revertant λ 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°C more stable than wild type. These two substitutions replace an α 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.
KW - differential scanning calorimetry
KW - mutant repressors
KW - protein stability
KW - thermal denaturation
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U2 - 10.1002/jcb.240290306
DO - 10.1002/jcb.240290306
M3 - Article
C2 - 4077930
AN - SCOPUS:0022308249
SN - 0730-2312
VL - 29
SP - 217
EP - 224
JO - Journal of supramolecular structure and cellular biochemistry
JF - Journal of supramolecular structure and cellular biochemistry
IS - 3
ER -