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Synopsis

Collagen is the most abundant protein in humans. A single collagen molecule forms a right-handed triple helix from three left-handed protein chains. These helices assemble into fibrils that provide mechanical strength to tissues such as bone, tendon, and skin. In this presentation, I will show atomic force microscopy (AFM) images of individual collagen molecules. I trace their contours and analyze conformations to determine persistence length, a measure of molecular stiffness. These results offer insight into collagen mechanics at the single-molecule level and lay the groundwork for resolving finer structural features such as helical pitch. Other techniques, including X-ray crystallography, have revealed atomic-level structure only for short collagen-like peptides; full-length single collagen molecules remain unresolved. AFM offers an alternative approach with the potential to directly visualize the helical pitch. Ultimately, this work helps connect molecular structure to mechanical properties in our connective tissues. Such insights support broader efforts to understand collagen-related genetic disorders such as brittle bone disease and Ehlers-Danlos syndrome.