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Additionally, all of the mutant structures reveal a reduced mobility in the catalytic histidine, providing further explanation for the loss of catalytic activity.
As expected, many (though not all) of the mutant p53 mouse models are susceptible to enhanced spontaneous and carcinogen-induced tumors of a variety of types.
Although the majority were TS for function in vivo, all of the mutant enzymes were stably expressed and largely soluble at both 30 degrees C and 42 degrees C in vivo and none of the mutants was found to be TS in vitro.
These primers surrounded all of the mutant alleles and therefore diagnosis was done in a multiplex PCR reaction.
All of the mutant alleles are inherited as dominant with incomplete penetrance (see Figure S1 and Table 1).
A dose dependent decrease in survival was observed for all of the mutant strains with the recombination deficient strains demonstrating the greatest sensitivity to DOX.
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Moreover, all of the mutants showed greater substrate affinity and kcat/Km than the native Srxyn.
The resistance towards thermal inactivation at alkaline pH was increased in all of the mutants.
All of the mutants display sigmoidal thermal unfolding and urea-induced unfolding curves.
Using differential scanning calorimetry to determine the relative stabilities of the wild-type and mutant proteins, we found all of the mutants to be destabilizing.
Using an HIV-1 cell fusion assay, we show that all of the mutants inhibit HIV-1 fusion with nearly identical IC50 values as wild-type CVN.
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