Recent data suggest hydrophobic interactions could be the main contributor.

This is a strong indication that electrostatic and hydrophobic interactions can be similarly affected by changes in temperature.

The subunits are held together through extensive hydrogen-bonding and hydrophobic interactions.

Another twenty years had to pass before hydrophobic interactions were recognized as the chief driving force in protein folding.

The interface between the two monomers is formed through hydrogen bonds and hydrophobic interactions.

Now it is recognized as an important link in hydrophobic interaction with capsaicin.

The enzyme's compact, globular structure results from significant hydrophobic interactions between these two domains.

For example, hydrophobic interactions can cause membrane proteins to aggregate during purification.

The bioimmobilization can also be performed via hydrophobic interactions between the molecule and the surface.

Overall, hydrophobic interactions are the major driving force in the formation of lipid bilayers.