Forces Maintaining the Stability of Tertiary Structure
The tertiary structures of proteins are stabilized by intermolecular forces; the hydrophobic effect, hydrogen bonds, ionic interactions, and London dispersion forces all contribute. The relative contribution of these forces has been quantified. More recently, the strategies employed by thermophilic proteins, which allow them to maintain their structures at extreme temperatures, have been identified. A growing appreciation of the need for some proteins to change their tertiary structure has developed, and the factors which allow them to adopt radically different folds are being identified.
In order to understand both the stability of protein structure and also their inherent plasticity, it is necessary to understand the transient forces that fold and hold the linear protein chain into a three-dimensional shape. Although these forces are often within an...