logo.gif (3296 bytes)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:

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":
  

 

 

Key:: Hydrophobic, Hydrophilic

 

Slab mode allows us to "slice" through the middle of a protein.

The menu 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%.


Copyright 1998, 1999, 2007 by Frank R. Gorga;   Page maintained by F.R. Gorga;   Last updated: 12-Mar-2007