Presented at the New Swiss Chemical Society (NSCS) Fall Meeting, University of Lausanne, 15 October 1997.
(Abstract published in Chimia, 1997, 51, 646)


Physical Chemistry, Poster 230

Entropy of Mixing, Hydrophobic Effect and Protein Folding

Shu-Kun Lin

MDPI Center, Sängergasse 25, CH-4054, Basel (Lin@mdpi.org)

A new theory of entropy of mixing that entropy of mixing or entropy of assembling increases continuously with the increase in the similarity of the components, has been developed based on the abandoning of the conventional statistical mechanics theory of mixing process [1-3]. This theory has given a perfect explanation of the process spontaneity of the hydrophobic effect and the protein folding phenomena. It also provided foundation for quantitative calculation of changes of thermodynamic parameters, particularly entropy and free energy.

Acknowledgments: This work has been performed at ETH-Zürich and in Basel. The author is grateful to Professor B. Jaun (ETH-Zürich) and Dr. V. Rassetti (Ciba-Geigy AG) for their kind supports.

References

[1] S.-K. Lin, J. Chem. Inf. Comp. Sci. 1996, 36, 367-376.

[2] S.-K. Lin, J. Theor. Chem. 1996, 1, 135-150.

[2] S.-K. Lin, Theochem 1997, in press.