We introduce a quantity, the entropic susceptibility, that measures the thermodynamic importance—for the folding transition—of the contacts between amino acids in model proteins. Using this quantity, we find that only one equilibrium run of a computer simulation of a model protein is sufficient to select a subset of contacts that give rise to the peak in the specific heat observed at the folding transition. To illustrate the method, we identify thermodynamically important contacts in a model 46-mer. We show that only about 50% of all contacts present in the protein native state are responsible for the sharp peak in the specific heat at the folding transition temperature, while the remaining 50% of contacts do not affect the specific heat.
|Original language||English (US)|
|Journal||Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics|
|State||Published - 2001|
All Science Journal Classification (ASJC) codes
- Statistical and Nonlinear Physics
- Statistics and Probability
- Condensed Matter Physics