.png){kind=icon}
.png){kind=icon}
Return
Classical and Modern Differential Scanning Calorimetry of Proteins: Integrating Equilibrium Thermodynamics with Emerging Diagnostic and Pharmaceutical Applications
.png){kind=icon}
PRE
AI
M
A
M
M
H
DOI：10.1016/j.pbiomolbio.2026.03.007.png)
.png){kind=icon}
Original request for help.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
Differential scanning calorimetry (DSC) remains a cornerstone technique for quantifying protein stability, unfolding cooperativity, and thermodynamic reversibility. While the classical calorimetric framework—rooted in excess heat-capacity analysis, transition enthalpy, and baseline construction—has been firmly established for decades, recent advances have expanded the scope of DSC toward complex biological systems and translational applications. These include ligand binding and screening, plasma thermogram profiling for disease-associated perturbations, high-sensitivity microcalorimetry, and cautiously applied data-driven signal deconvolution approaches. In this work, we revisit the thermodynamic foundations of protein DSC with a critical focus on cooperativity ratios, reversibility criteria, and heat-capacity changes, emphasizing their continued relevance in modern contexts. Particular attention is given to baseline construction and its quantitative impact on enthalpy determination, highlighting practical limitations, sources of uncertainty, and error bounds. Classical stability parameters are then discussed in relation to emerging applications, illustrating how rigorous calorimetric analysis can support contemporary uses of DSC in biopharmaceutical characterization, molecular diagnostics, and integrative biophysical studies. Rather than proposing a new formal or universal theory, this article synthesizes established thermodynamic principles into a comparative and conditional analytical perspective that offers a comparative perspective that connects classical methodology with current and evolving DSC applications
Keywords:
Protein stability
Differential scanning calorimetry
Thermodynamic reversibility
Cooperativity ratios
Biopharmaceutical characterization
Journal
IF:
4.5
Papers:
1.8K
Citations:
4.7K
Organization
Cited Papers