Structure and Mechanical Properties of Rubberlike Proteins in Animals

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Abstract
Polymer networks formed from protein molecules that adopt kinetically-free, random-coil conformations are found in many animals, where they play a number of important roles. The 5 rubberlike proteins isolated and studied to date indicate that animal rubbers, like their synthetic counterparts, contain random networks which are usually stabilized by covalent crosslinks. Long-range elasticity in rubberlike proteins is based on changes in the conformational entropy of random-coil molecules. Further, these protein networks show viscoelastic glass transitions similar to all other amorphous polymer networks. Future research on protein sequences should increase our understanding of how polypeptide chains can function as random-coil molecules, and studies into the mechanical state of elastin in arterial tissues may provide important clues about the mechanisms of some forms of human disease.

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