Recent studies demonstrated that Gaussian accelerated molecular dynamics (GaMD) is a robust computational technique, which provides simultaneous unconstrained enhanced sampling and free energy calculations of biomolecules. However, the exact acceleration of biomolecular dynamics or speedup of kinetic rates in GaMD simulations and, more broadly, in enhanced sampling methods, remains a challenging task to be determined. Here, the GaMD acceleration is examined using alanine dipeptide in explicit solvent as a biomolecular model system. Relative to long conventional molecular dynamics simulation, GaMD simulations exhibited ∼36-67 times speedup for sampling of the backbone dihedral transitions. The acceleration depended on level of the GaMD boost potential. Furthermore, Kramers' rate theory was applied to estimate GaMD acceleration using simulation-derived diffusion coefficients, curvatures and barriers of free energy profiles. In most cases, the calculations also showed significant speedup of dihedral transitions in GaMD, although the GaMD acceleration factors tended to be underestimated by ∼3-96 fold. Because greater boost potential can be applied in GaMD simulations of systems with increased sizes, which potentially leads to higher acceleration, it is subject to future studies on accelerating the dynamics and recovering kinetic rates of larger biomolecules such as proteins and protein-protein/nucleic acid complexes.