Although extensive studies of collagen viscoelastic properties have been pursued at the macroscopic (fiber/tissue) level, fewer investigations have been performed at the smaller scales, including collagen molecules and fibrils. Here, using an atomistic modeling approach, we perform in silico creep tests of a collagen-like peptide, monitoring the strain-time response for different values of applied external load. The results show that individual collagen molecules exhibit a nonlinear viscoelastic behavior, with a Young's modulus increasing from 6 to 16 GPa (for strains up to 20%), a viscosity of 3.84.±0.38 Pa s, and a relaxation time in the range of 0.24-0.64 ns. Additionally, the mechanism for molecular sliding between collagen fibrils was studied by shearing the center molecule in a hexagonally packed bundle with varied lateral distance between the molecules. In dry conditions, the central molecule slid with a stick-slip mechanism that corresponded with the breaking and reformation of hydrogen bonds between collagen molecules. This mechanism was observed at varying shear velocities and at different lateral separations between molecules. In water and at small intermolecular lateral distances, the slip-stick behavior was also observed but above the threshold of 13 A lateral separation, the molecules sheared smoothly in water. Moreover, the average force required to shear remained the same in water as in vacuum, which suggests that the effect of water at this level is to mediate the transfer of load between molecules. Based on our molecular modeling results we propose a simple structural model that describes collagen tissue as a hierarchical structure, providing a bottom-up description of elastic and viscous properties form the properties of the tissue basic building blocks.