Hi all, this might be a silly question. But I am wondering if there are solvent molecules in the core of a protein where hydrophobic interactions are primary. We all know that water or general solvent molecules are polar. Polar molecules (solvent molecules) in the hydrophobic surroundings are considered to be unfavorable due to less entropy.. In a real world, is there an absolute absence of water molecules in the core of protein? or what are some things that can allow water molecule penetration into the core of a protein?
You know that a protein molecule is in a state of spiral and coil. This is due to the desire to minimize the Gibbs energy of the system. We simplify the explanation of the problem. Let us consider the change in the mean force potential W (r) between two methane molecules in water. It turns out that the potential has two minima: one at the contact of molecules, and the other at a distance of the diameter of the molecule of water (solvent). These are the molecules of water that penetrate the protein. See our work with this problem for surfactants.
Best regards.
Yes, there can be water in the core.
https://goo.gl/jwLFVh
This book has a nice description about it
https://goo.gl/Cj2u8F
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