Elastomeric proteins such as elastin, resilin, abductin and wheat gluten, which are evolutionarily unrelated, nevertheless share similar sequence features imparting their remarkable abilities to extend and recoil. In the absense of detailed structural information, rendering these sequence features challenging to study, we have undertaken a theoretical study examining the influence of domain arrangement on polymer assembly and integrity using a novel simulation environment.
This model uses diffusion limited aggregation to simulate the self-assembly of rod-like particles with alternating domain architectures such as those found in elastomeric proteins. These results demonstrate that elastomeric and cross-linking domains can significantly impact the morphology and structural integrity of the resulting aggregate structures leading to insights into the evolution of elastomeric proteins as well as providing a potentially useful tool to further investigate how molecules can be tuned for use in novel biomaterials.
Song, H. and Parkinson, J. (2012) Modelling the self-assembly of elastomeric proteins provides insights into the evolution of their domain architectures. PLoS Computational Biol. 8(3): e1002406