Inter-residue interactions in membrane proteins

Knowing the precise 3D-structure of a protein is crucial to understand its functional mechanism at the molecular level and to develop new pharmacological agents to targeting it. Nowadays only a few hundred integral membrane protein structures have been solved at high resolution due to the associated technical difficulties. In the present study we aim to characterize the main interactions in alpha and beta membrane proteins that are responsible of the maintenance of the overall structure. With this purpose, two nonredundant databases of alpha and beta transmembrane segments were constructed and analysed. The interactions that stabilize the structure of alpha and beta membrane proteins were quantified. The results reveal important differences in inter-residues interactions between alpha and beta membrane proteins. This novel structural information may be useful in predicting 3D models of proteins lacking structural information or in refining initial models of alpha and beta membrane proteins.