Magnetic resonance transverse spin relaxation time constants (T-2) of water protons in ordered collagenous tissues are dependent on the orientation of the tissue relative to the static magnetic field. This dependence is commonly referred to as the magic angle (MA) effect and has been attributed to the restricted rotational motion of icelike water bridges in the hydrated triple-helix collagen molecule. Understanding of the molecular mechanism of the MA effect is important for clinical and research applications of magnetic resonance spectroscopy and imaging to tissues, such as articular cartilage, tendons, and ligaments. In this work, we have used molecular dynamics simulations to investigate the subnanosecond time scale dynamics of single-water bridges in a model collagen peptide. We ascertain the residence times and the patterns of restricted rotational motion of water molecules. The key findings are strongly anisotropic rotation patterns of water molecules at bridge sites and a dynamic, rather than icelike, nature of the single-water bridges within the individual triple-helix collagen molecule.