Related Experiment Video
Updated: Jan 11, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Partition Function Zeros and Heat Capacity Decomposition Reveal HP Protein Foldability
Sing-Shuo Huang1, Chi-Ning Chen1
1Department of Physics, National Dong-Hwa University, Hualien 97401, Taiwan.
None:
The heat capacity decomposition method, a well-established analytical approach in polymer thermodynamics for elucidating thermal transitions in homogeneous polymers, is extended here to heterogeneous systems. We demonstrate that the decomposition of heat capacity based on partition function zeros allows the identification of transition-like crossovers originating from compact low-energy states, thereby enabling the evaluation of the foldability of HP sequences. The occurrence of significant crossovers between the collapse and folding transitions indicates slow folding behavior, whereas their absence characterizes good folders. This criterion is further validated through kinetic Monte Carlo simulations of two representative sequences.
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

