This repository provides a mean-field framework for fitting and analyzing protein folding experiments in the presence of cosolutes or crowders. Unlike conventional models limited to volume exclusion and protein–cosolute interactions, our approach also accounts for cosolute–solvent non-ideal mixing effects. The theoretical background is detailed in the accompanying notebook, which includes a step-by-step example demonstrating how to apply the model to experimental data.
If you use this model (in its original or modified form), please cite the following:
- Olgenblum, Gil I., Neta Carmon, and Daniel Harries. "Not always sticky: Specificity of protein stabilization by sugars is conferred by protein–water hydrogen bonds." Journal of the American Chemical Society 145.42 (2023): 23308-23320.
- Sapir, Liel, and Daniel Harries. "Macromolecular stabilization by excluded cosolutes: mean field theory of crowded solutions." Journal of chemical theory and computation 11.7 (2015): 3478-3490.
- Stewart, Claire J., et al. "Resolving the enthalpy of protein stabilization by macromolecular crowding." Protein Science 32.3 (2023): e4573.