Low-Frequency Cooperative Dynamics in l-, d-, and dl-Alanine Crystals: A 13C and 15N Cross-Polarization Magic-Angle-Spinning NMR Study

Abstract

Knowledge of the dynamical changes in molecular configurations in various amino acid structures over a wide range of time scales is important since such changes may influence the structural transformations and the diverse biological functionalities of proteins. Using the temperature dependence of the rotating-frame NMR spin-lattice relaxation times T(1rho) of protons as a probe, we have investigated the low-frequency (approximately 60-100 kHz) dynamics in the crystal structures of L-, D-, and DL- alanine (C(12)H(28)O(8)N(4)) polymorphs. The proton relaxation times T(1rho) were obtained from (13)C <-- (1)H and (15)N <-- (1)H cross-polarization magic-angle-spinning NMR experiments over a temperature range of 192-342 K. The data reveal that the time scales of these low-frequency dynamical processes are distinctly different from the localized, high-frequency rotational motion of methyl and amine groups. The strongly asymmetric T(1rho) versus temperature curves and the subtle dynamical differences between the DL-alanine and the L- and d-enantiomorphs indicate that these low-frequency processes are cooperative in nature and are sensitive to molecular packing.