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J. A. Schellmann, “The thermodynamics of urea solutions and the heat of Formation of the peptide hydrogen bond,” Compt. Rend. Lab. Carlsberg. Ser. Chim., 29, 223, 230 (1955).

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Article

Inversion of the Hydrophobic/Hydrophilic Paradigm Demystifies the Protein Folding and Self-Assembly of Problems

1Department of Physical Chemistry The Hebrew University of Jerusalem, Jerusalem, Israel


International Journal of Physics. 2013, Vol. 1 No. 3, 66-71
DOI: 10.12691/ijp-1-3-2
Copyright © 2013 Science and Education Publishing

Cite this paper:
Arieh Ben-Naim. Inversion of the Hydrophobic/Hydrophilic Paradigm Demystifies the Protein Folding and Self-Assembly of Problems. International Journal of Physics. 2013; 1(3):66-71. doi: 10.12691/ijp-1-3-2.

Correspondence to: Arieh Ben-Naim, Department of Physical Chemistry The Hebrew University of Jerusalem, Jerusalem, Israel. Email: arieh@fh.huji.ac.il

Abstract

The idea that the hydrophobic effect is the major driving force for processes such as protein folding and protein-protein association has prevailed in the biochemical literature for over half a century. It has recently become clear that the evidence in favor of the hydrophobic paradigm has totally dissipated. The dominance of the hydrophobic effect has been reduced into nothing but a myth. On the other hand, the new paradigm based on a host of hydrophilic effects has emerged. This new paradigm offers simple and straightforward answers to the long sought problems of protein folding and protein-protein association.

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