Investigation of the dynamical properties of water in elastin by deuterium Double Quantum Filtered NMR.

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. Copyright (c) 2010 Elsevier Inc. All rights reserved.