A layer of solvent which surrounds the protein can also help stabilize its confirmation. This is known as the solvation layer or solvation shell.
Proteins are in a stable confirmation when they are active. Upon denaturation, the protein is unfolded causing inactivation. In biological systems, proteins are constantly folding and unfolding to regulate their activity. Various factors that can cause protein denaturation are listed in the table below:
|High Temperature||Destroys 2°, 3°, 4° structure|
|pH (acids or bases)||Disruption of ionic bonds destroying 3°, 4° structure|
|Chemicals (eg: alcohol)||Generally disrupts hydrogen bonds destroying 2°, 3°, 4° structure|
|Enzymes||Breaks the individual peptide bonds destroying 1° structure|
The hydrophobic effect refers to the tendency for R-groups on amino acids to be pushed inward when surrounded by a solvent such as water. Hydrophilic groups move towards the solvent in the case of water. This effect allows the secondary structure of proteins to fold into tertiary structures. The solvent which surrounds the protein greatly affects its stability and confirmation.