Theoretical stress–strain isotherms for elastin model networks

A theoretical analysis was carried out for polypeptides composed exclusively of one of the three highly conserved repeat sequences present in the bioelastomer elastin. Conformational energy maps of the relevant amino acids were generated and a standard matrix method used. Various levels of intramolecular hydrogen bonding were studied, ranging from none to the inclusion of longer‐range hydrogen bonds implicated in stabilizing β‐bend conformations considered of importance owing to a Pro‐Gly pair present in each of the three repeat peptides. Monte Carlo techniques were used to evaluate the distribution functions of the end‐to‐end distance vector r , from which the modulus as a function of elongation was calculated. With minor exception, the resulting stress–strain isotherms for chains having degree of polymerization 5 and 10 showed little deviation from Gaussian behavior for elongation ratios up to 2.