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We report on the direct measurement of the correlation times of the proteinbackbone carbons and proximal waters of hydration in mechanically strainedelastin by nuclear magnetic resonance methods. The experimental data indicate adecrease in the correlation times of the carbonyl carbons as the strain on thebiopolymer is increased. These observations are in good agreement with short4ns molecular dynamics simulations of (VPGVG)3, a well studied mimetic peptideof elastin. The experimental results also indicate a reduction in thecorrelation time of proximal waters of hydration with increasing strain appliedto the elastomer. A simple model is suggested that correlates the increase inthe motion of proximal waters of hydration to the increase in frequency oflibration of the protein backbone that develops with increasing strain.Together, the reduction in the protein entropy accompanied with the increase inentropy of the proximal waters of hydration with increasing strain, support thenotion that the source of elasticity is driven by an entropic mechanism arisingfrom the change in entropy of the protein backbone.

Direct measurement of the correlated dynamics of the protein-backbone and proximal waters of hydration in mechanically strained elastin