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A simple model for determining affinity from irreversible thermal shifts.

ABSTRACT: Thermal denaturation (Tm) data are easy to obtain; it is a technique that is used by both small labs and large-scale industrial organizations. The link between ligand affinity (K _D ) and ΔTm is understood for reversible denaturation; however, there is a gap in our understanding of how to quantitatively interpret ΔTm for the many proteins that irreversibly denature. To better understand the origin, and extent of applicability, of a K _D to ΔTm correlate, we define equations relating K _D and ΔTm for irreversible protein unfolding, which we test with computational models and experimental data. These results suggest a general relationship exists between K _D and ΔTm for irreversible denaturation.

SUBMITTER: Hall J

PROVIDER: S-EPMC6739816 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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A simple model for determining affinity from irreversible thermal shifts.

Hall Justin J

Protein science : a publication of the Protein Society 20190812 10

Thermal denaturation (Tm) data are easy to obtain; it is a technique that is used by both small labs and large-scale industrial organizations. The link between ligand affinity (K <sub>D</sub> ) and ΔTm is understood for reversible denaturation; however, there is a gap in our understanding of how to quantitatively interpret ΔTm for the many proteins that irreversibly denature. To better understand the origin, and extent of applicability, of a K <sub>D</sub> to ΔTm correlate, we define equations r ...[more]

PMID: 31361943

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