Tropoelastin is a protein, of size 72kDa, that comes together via cross-links to form elastin in the extracellular matrix of the cell. The cross-link formation process is mediated by lysyl oxidase.  One of the major reasons that elastin can withstand high levels of stress in the body without experiencing any physical deformation is that the underlying tropoelastin contains domains that are highly hydrophobic. These hydrophobic domains, consisting overwhelmingly of alanine, proline, glycine, and valine, tend towards instability and disorderliness, ensuring that the elastin does not lock into any specific confirmation.  Thus, ELPs consisting of the Val-Pro-Gly-X-Gly monomeric units, which bear resemblance to the repetitive tropoelastin hydrophobic domains, are highly disordered below their T  Even above their T in their aggregated state, ELPs are only partially ordered. This is due to the fact that the proline and glycine amino acids are present in high amounts in the ELP.  Glycine, due to the lack of a bulky side chain, enables the biopolymer to be flexible and proline prevents the formation of stable hydrogen bonds in the ELP backbone.  It is important to note, however, that certain segments of the ELP may be able to form instantaneous type II β turns, but these turns are not long-lasting and do not resemble true β sheets, when the NMR chemical shifts are compared.