Zeitschrift für Proteomik und Bioinformatik
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Self-Assembly of Open Protein Systems: A Comprehensive View Based onthe Interactions between 3d Hydrophobic and Electric Dipole MomentVectors

Angel Mozo-Villarías, Juan A Cedano and Enrique Querol

One of the most important phenomena in biology and medicine is protein self-assembly. In previous studies we mostly considered closed assemblies with a finite number of components. This article further explores self-assemblies involving an indeterminate number of components or open systems. In spite of the great variety of sizes, shapes and functions that self-assembled complexes of proteins are present in nature, they all seem to obey a relative simple law regarding their hydrophobic interactions. This law can be stated in very simple terms with the help of the definition of the hydrophobic moment vector applied to the double layer of phospholipids in biological membranes as a model. Simply stated, proteins assemble by tending to align their hydrophobic moments vectors, H. The reason that only a few examples of assemblies show a perfect alignment of their H vectors is due to the modifying action of their electrostatic interactions by means of their electric dipole moments, D. This principle works in all scales of protein sizes and allows higher-order assemblies, that is, assemblies of assemblies.