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- W4211263644 abstract "P53 is a tumor suppressor and transcription factor that is stabilized and activated by cellular stress. P53 contains a disordered transactivation domain (TAD) (residues 1-40) that becomes helical at residues 19-25 when bound to its inhibitors, MDM2 and MDMX. Previous studies from our lab have shown that increasing the transient helicity of p53TAD using mutagenesis increased the affinity with MDM2. We hypothesized this was due to a reduction in the entropic penalty of coupled folding and binding." @default.
- W4211263644 created "2022-02-13" @default.
- W4211263644 creator A5042691692 @default.
- W4211263644 date "2022-02-01" @default.
- W4211263644 modified "2023-09-26" @default.
- W4211263644 title "Measuring the energetic penalty of folding and binding between p53 and MDM2" @default.
- W4211263644 doi "https://doi.org/10.1016/j.bpj.2021.11.2426" @default.
- W4211263644 hasPublicationYear "2022" @default.
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