Study of strong to ultratight protein interactions using differential scanning calorimetry.

@article{Brandts1990StudyOS,
  title={Study of strong to ultratight protein interactions using differential scanning calorimetry.},
  author={John F Brandts and Li-yang Lin},
  journal={Biochemistry},
  year={1990},
  volume={29 29},
  pages={6927-40}
}
Data from differential scanning calorimetry (DSC) may be used to estimate very large binding constants that cannot be conveniently measured by more conventional equilibrium techniques. Thermodynamic models have been formulated to describe interacting systems that involve either one thermal transition (protein-ligand) or two thermal transitions (protein-protein) and either 1:1 or higher binding stoichiometry. Methods are described for obtaining binding constants and heats of binding by two… CONTINUE READING
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