What are the underlying principles of hydrophobicity at the molecular level?

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Hydrophobicity at the molecular level, particularly concerning amino acids, is primarily driven by entropic processes, as highlighted by the Gibbs free energy equation. The discussion seeks more comprehensive resources beyond basic wiki articles, emphasizing a need for references that delve into statistical mechanics rather than just thermodynamics. A couple of articles were shared that provide insights into this topic, but there is a desire for deeper exploration and understanding. The community is encouraged to contribute additional findings or references that expand on these principles. A thorough examination of hydrophobic interactions remains a valuable pursuit in molecular physics.
dipole
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Hi, I'm looking for a good reference on the physics of hydrophobicity on the level of molecules. I'm specifically interested in amino acids, but I'd prefer a more general discussion.

The wiki articles are pretty slim, so hoping someone here might have a better resource. Thanks.
 
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I'm sorry you are not generating any responses at the moment. Is there any additional information you can share with us? Any new findings?
 
I found this article cited by the wiki: http://pubs.acs.org/doi/abs/10.1021/ed075p116

which has a reference to this one: http://pubs.acs.org/doi/pdf/10.1021/ed066p581

The basic message I took from the above is that hydrophobic interactions are mostly driven by entropic processes - i.e. the "TΔS" term in the Gibbs free energy. I stopped at this point, but it would be cool to see a more in-depth discussion, and one which is written perhaps from a more statistical mechanics point of view rather than just pure thermodynamics and some handwaving.
 
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