Entropic elastomeric force in protein structure/function

Briefly noting earlier studies on the polypentapeptide of elastin, (Val 1 ‐Pro 2 ‐Gly 3 ‐Val 4 ‐Gly 5 ) n , and on elastin, it is emphasized that entropic elastomeric force can be exhibited by nonrandom, anisotropic polypeptide systems and therefore that entropic elastomeric force does not necessarily result from isotropic random chain networks as required by the classical theory of rubber elasticity, nor does it result from solvent entropy effects as deduced from the slow loss of elastomeric force on thermal denaturation. Instead entropic protein elasticity can be the result of internal chain dynamics, specifically of librational processes that become damped on chain extension. This new mechanism of entropic protein elasticity allows for an understanding not only of elastin but also of the passive tension of striated muscle, of the voltage‐dependent interconversion between open and closed conductance states in the sodium channel of squid nerve, and of protein elastic forces producing strain in a substrate bond during enzyme catalysis. Because entropic elastomeric force develops as a result of an inverse temperature transition, it becomes possible to shift the temperature of the transition to higher or lower temperatures by decreasing or increasing, respectively, the hydrophobicity of the elastomeric polypeptide chain. In warm‐blooded animals this allows for biochemical modulation of the relaxation or development of entropic elastomeric force by an enzymatically modulated decrease or increase of the hydrophobicity, as for example, by phosphorylation or dephosphorylation of the elastomeric polypeptide chain. This understanding provides a mechanism for modulating protein function, whether for example enzymatic or channel, a mechanism for the remarkable reversible structural processes that attend parturition, and a mechanism for the connective tissue anomalies of wound repair and enviromentally induced lung disease.