Hydrophobic Effect

Introduction to Protein Structure

The Hydrophobic Effect

The "hydrophobic effect" (a term coined by Charles Tanford) refers to the idea that energetically protein folding is driven by two factors:

Hydrophobic (or "oily") groups "prefer" to "get away" from water
Hydrophilic groups "prefer" to "dissolve" in the water.

Thus, most globular proteins consist of a core composed mainly of hydrophobic residues surrounded by a "skin" composed mainly of hydrophilic residues.

This can be seen in the molecular model of lysozyme shown here:

Notice how the hydrophilic residues, generally form a "ring" around a core of mostly hydrophobic residues.		Plane of "slice"
		20%	30%
		40%	50%
		60%	70%
		80%	90%
		100%

	Key:: Hydrophobic, Hydrophilic
Slab mode allows us to "slice" through the middle of a protein. Clicking on the buttons to the right of the model changes the "depth" of the slice. (0% would be the back of the molecule; 100% is the complete molecule). The inital setting is 50%.