Abstract
We report solid‐state NMR investigations of the effect of temperature and hydration on the molecular mobility of collagen isolated from bovine achilles tendon. ^13^C cross‐polarization magic angle spinning (MAS) experiments were performed on samples at natural abundance, using NMR methods that detect motionally averaged dipolar interactions and chemical shift anisotropies and also slow reorientational processes. Fast motions with correlation times much shorter than 40 µs scale dipolar couplings and chemical shift anisotropies of the carbon sites in collagen. These motionally averaged anisotropic interactions provide a measure of the amplitudes of the segmental motions expressed by a molecular order parameter. The data reveal that increasing hydration has a much stronger effect on the amplitude of the molecular processes than increasing temperature. In particular, the Cγ carbons of the hydroxyproline residues exhibit a strong dependence of the amplitude of motion on the hydration level. This could be correlated with the effect of hydration on the hydrogen bonding structure in collagen, for which this residue is known to play a crucial role. The applicability of 1D MAS exchange experiments to investigate motions on the millisecond time‐scale is discussed and first results are presented. Slow motions with correlation times of the order of milliseconds have also been detected for hydrated collagen. Copyright © 2004 John Wiley & Sons, Ltd.