We report a new solid-state multidimensional NMR approach based on the cross-polarization with variable-contact pulse sequence [Paluch, P.; Pawlak, T.; Amoureux, J.-P.; Potrzebowski, M. J. J. Magn. Reson. 233, 2013, 56], with H-1 inverse detection and very fast magic angle spinning (v(R) = 60 kHz), dedicated to the measurement of local molecular motions of H-1-N-15 vectors. The introduced three-dimensional experiments, H-1-N-15-H-1 and hCA(N)H, are particularly useful for the study of molecular dynamics of proteins and other complex structures. The applicability and power of this methodology have been revealed by employing as a model sample the GB-1 small protein doped with Na(2)CuEDTA. The results clearly prove that the dispersion of H-1-N-15 dipolar coupling constants well correlates with higher order structure of the protein. Our approach complements the conventional studies and offers a fast and reasonably simple method.