Mobility of elastin chains as determined by 13C nuclear magnetic resonance |
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Authors: | D A Torchia K A Piez |
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Affiliation: | National Bureau of Standards Polymer Crystal Physics Section Washington, D. C. 20234, U.S.A.;Laboratory of Biochemistry National Institute for Dental Research Bethesda, Md 20014, U.S.A. |
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Abstract: | Relaxation times and integrated intensities of 13C have been obtained from nuclear magnetic resonance spectra of elastin in unstretched calf ligamentum nuchae and indicate that about 80% of the backbone carbonyl carbons have short rotational correlation times, τR ~ 40 nanoseconds. τR is reduced by only a factor of two when the ligament is in contact with 2 m-KCNS, a strong denaturant. By contrast, the highly ordered chains of collagen in insoluble calf achilles tendon give no spectrum until denatured in 2 m-KCNS, when tR decreases by many orders of magnitude. These results show that elastin is composed largely of highly mobile chains under physiological conditions, suggesting that configurational entropy has an important role in its elastic properties. |
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