Protein found in a biological system with a unique three-dimensional structure and biological activity is called a native protein. When a protein in its native form, is subjected to physical change like change in temperature or chemical change like change in pH, the hydrogen bonds are disturbed. Due to this, globules unfold and helix get uncoiled and protein loses its biological activity. This is called denaturation of protein. During denaturation secondary and tertiary structures are destroyed but primary structure remains intact. The coagulation of egg white on boiling is a common example of denaturation.

Which of the following forces is favorable for protein folding?

Hydrophobic interactions

Hydrophobic interactions aids in keeping protein stable and biologically active by allowing the protein to reduce its surface area.