References

Citations and bibliography for papers and resources used by this project.

[1]

J. Duan, D. Lupyan, and L. Wang. Improving the accuracy of protein thermostability predictions for single point mutations. Biophysical Journal, 119:115–127, 2020.

[2]

V. Gapsys, S. Michielssens, D. Seeliger, and B. L. de Groot. Accurate and rigorous prediction of the changes in protein free energies in a large–scale mutation scan. Angewandte Chemie International Edition, 55:7364–7368, 2016.

[3]

D. Seeliger and B. L. de Groot. Protein thermostability calculations using alchemical free energy simulations. Biophysical Journal, 98:2309–2316, 2010.

[4]

R. L. Hayes, J. Z. Vilseck, and C. L. Brooks III. Approaching protein design with multisite λ dynamics: accurate and scalable mutational folding free energies in t4 lysozyme. Protein Science, 27:1910–1922, 2018.

[5]

R. W. Zwanzig. High–temperature equation of state by a perturbation method. i. nonpolar gases. The Journal of Chemical Physics, 22:1420–1426, 1954.

[6]

J. G. Kirkwood. Statistical mechanics of fluid mixtures. J. Chem. Phys., 3:300–313, 1935.

[7]

R. L. Hayes, K. A. Armacost, J. Z. Vilseck, and C. L. Brooks III. Adaptive landscape flattening accelerates sampling of alchemical space in multisite λ dynamics. J. Phys. Chem. B, 121:3626–3635, 2017.