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Protein folding consists of a balance between a substantial amount of weak intra-molecular interactions within a protein (Hydrophobic, electrostatic, and Van Der Waals Interactions) and protein-solvent interactions. As a result, this process is heavily reliant on environmental state that the protein resides in. These environmental conditions include, and are not limited to, temperature, salinity, pressure, and the solvents that happen to be involved. Consequently, any exposure to extreme stresses (e.g. heat or radiation, high inorganic salt concentrations, strong acids and bases) can disrupt a protein's interaction and inevitably lead to denaturation.

Misfolding Due to Heavy Metals and Metalloids

By targeting proteins, heavy metals have been known to disrupt the function and activity carried out by proteins. It is important to note that heavy metals fall into categories consisting of transition metals as well as a select amount of metalloid. These metals, when interacting with naive, folded proteins, tend to play a role in obstructing their biological activity. This interference can be carried out in a different amount of ways. These heavy metals can form a complex with the functional side chain groups present in a protein or form bonds to free thiols. Heavy metals also play a role in oxidizing amino acid side chains present in protein. Along with this, when interacting with metalloproteins,heavy metals can dislocate and replace key metal ions. As a result of these interferences, heavy metals can strongly affect protein stability and activity.

By targeting proteins, heavy metals have been known to disrupt the function and activity carried out by proteins. It is important to note that heavy metals fall into categories consisting of transition metals as well as a select amount of metalloid. These metals, when interacting with naive, folded proteins, tend to play a role in obstructing their biological activity. This interference can be carried out in a different amount of ways. These heavy metals can form a complex with the functional side chain groups present in a protein or form bonds to free thiols. Heavy metals also play a role in oxidizing amino acid side chains present in protein. Along with this, when interacting with metalloproteins, heavy metals can dislocate and replace key metal ions. As a result, heavy metals can interfere with folded proteins, which can strongly deter protein stability and activity.