Premium
A simple model for determining affinity from irreversible thermal shifts
Author(s) -
Hall Justin
Publication year - 2019
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3701
Subject(s) - denaturation (fissile materials) , simple (philosophy) , chemistry , thermodynamics , ligand (biochemistry) , scale (ratio) , thermal , biological system , crystallography , physics , biology , biochemistry , philosophy , receptor , epistemology , nuclear chemistry , quantum mechanics
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 Δ Tm is understood for reversible denaturation; however, there is a gap in our understanding of how to quantitatively interpret Δ Tm for the many proteins that irreversibly denature. To better understand the origin, and extent of applicability, of a K D to Δ Tm correlate, we define equations relating K D and Δ Tm for irreversible protein unfolding, which we test with computational models and experimental data. These results suggest a general relationship exists between K D and Δ Tm for irreversible denaturation.