The anisotropic motion of tightly bound waters of hydration in bovine nuchal ligament elastin has been studied by deuterium Double Quantum Filtered (DQF) NMR. The experiments have allowed for a direct measurement of the degree of anisotropy within pores of elastin over a time scale ranging from 100 micros to 30 ms, corresponding to a tortuous spatial displacement ranging from 0.2 to 7 microm. We studied the anisotropic motion of deuterium nuclei in D2O hydrated elastin over a temperature of -15 degrees C to 37 degrees C and in solvents with varying dielectric constants. Our experimental measurements of the residual quadrupolar interaction as a function of temperature are correlated to the existing notion of hydrophobic collapse near 20 degrees C.
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| http://dx.doi.org/10.1016/j.jmr.2010.04.007 | DOI Listing |
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