Tools and Data Sets
Modelling the Self-assembly of Elastomeric Proteins
Elastomeric proteins have evolved independently multiple times through evolution. Produced as monomers, they self-assemble into polymeric structures that impart properties of stretch and recoil. They are composed of an alternating domain architecture of hydrophobic domains, which in addition to providing the elasticity help drive the assembly process, interspersed with cross-linking elements, which help stabilise the polymer. Changes in the
number and arrangement of the hydrophobic and cross-linking regions can significantly impact their assembly and mechanical properties. However such studies exploring the functional consequences of changes in the arrangement of hydrophobic and cross-linking elements have been limited. Here we present a theoretical study that examines the impact of domain architecture on polymer assembly and integrity. At the core of this study is a novel simulation environment that uses a model of Diffusion-limited aggregation to simulate the self-assembly of rod-like molecules with alternating domain architectures. Applying the model to different domain architectures, we generate a variety of aggregates which are subsequently analysed by graph-theoretic metrics to predict their structural integrity.
Click here to download the source of the simulation package. Before you run the program, please click and read the introduction.
