Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation.

@article{Lepock1992InfluenceOT,
  title={Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation.},
  author={James R. Lepock and K P Ritchie and Michael C. Kolios and A M Rodahl and Karl Heinz and J A Kruuv},
  journal={Biochemistry},
  year={1992},
  volume={31 50},
  pages={12706-12}
}
The thermodynamic parameters characterizing protein folding can be obtained directly using differential scanning calorimetry (DSC). They are meaningful only for reversible unfolding at equilibrium, which holds for small globular proteins; however, the unfolding or denaturation of most large, multidomain or multisubunit proteins is either partially or totally irreversible. The simplest kinetic model describing partially irreversible denaturation requires three states: Formula [see text] We… CONTINUE READING

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