There exists a great deal of information concerning lipid structures, but a limited amount of direct structural information is available on membrane proteins. In particular, the effects of bilayer physicochemical properties on protein structure and function are anticipated to give further insight in membrane functioning. The regulatory effect of hydrophobic thickens of lipid bilayer on protein functioning. The effect of protein secondary structures on the ion channel activity. The influence of bilayer lateral pressure on the activity of membrane enzymes or conducting properties of membrane ion channels.
Most biological processes demand a concerted action of more than one protein.
In the biological membrane there are several processes where protein-protein recognition plays a very important role. For instance, making a channel, insertion of proteins in the membrane, assembly of enzymes, assembly of electron transport chains, and phage assembly. Recent theoretical and experimental studies have started to address the fundamental problem of how proteins recognise each other, and which molecular forces are involved. However, more effort should be directed towards amino acid motifs that are important for dimer or oligomer formation, and the importance of hydrophobic and electrostatic interactions between proteins. An important contribution to the understanding of processes that lead to the aggregation of the proteins in the membrane came from simulation work using Monte Carlo simulations on model membrane systems.