Through a nuanced balance of electrical and hydrophobic forces, biological molecules self-assemble into the large functional structures that maintain life's vital functions. Understanding how proteins self-assemble requires knowledge of both forces. But while predicting the electrical interactions of individual proteins is simple, deriving their hydrophobic ones is less straightforward.
, Angel Mozo-Villarias, of the Autonomous University of Barcelona, Spain, and his colleagues develop a formulation for how proteins align into membrane-like structures based on. The model could help to predict the configuration of macromolecular assemblies at any scale, providing a useful tool for novel materials and drug discovery research.
Hydrophobicity is an emergent property of complex molecular systems that does not manifest itself in each individual component. To examine hydrophobicity in proteins, researchers assign each of their constituent amino acids an index on a scale according to how much energy it takes to transfer them from a hydrophilic medium to a hydrophobic one.
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