DescriptionCollagen is an abundant and integral protein within the body, due to its mechanical strength and elasticity. These properties arise from the structural hierarchy of collagen, from the peptide strands, to tropocollagen, to microfibrils, to fibers. Understanding the formation mechanisms of collagen can aid in the research of various collagen related disorders, such as heart disease, skin aging, Osteogenesis Imperfecta, etc. In this study, we simulated three short, simplified collagen peptide strands using the MARTINI coarse grained scheme. Once the tropocollagen was formed, it was replicated five more times and simulated to form a microfibril. Using mathematical equations of a helix, we characterized the tropocollagen to have a curvature (κ) of 0.9237 and a torsion (τ) of 0.6395. The maximum average interaction count occurs between two of the three strands for the tropocollagen at fifteen, suggesting in partial uncoiling of the triple helix. The average interaction counts for the microfibril are around eight, suggesting that the formation mechanism is the individual peptide strands bundling to form a microfibril-like structure, rather than forming tropocollagensand then microfibris.