Abstract
Research concentrated around the extracellular matrix (ECM) and its tissue mechanics maintains prevalence in the biophysics area. A key player in the human connective tissue is type I collagen fibrils which make up a significant portion of the interstitial matrix, basement membranes, and the bone matrix. The formation of fibrils depends largely on individual collagen molecules and assumedly the amino acids that compose each helix in type I tropocollagen. Comprehensive examination of the flexibility within individual type I collagen molecules has not yet been completed. We have used atomic force microscopy to image and retrieve objective statistical data about deviations from the natural curvature in the molecule. This information will allow us to find the ranges in which the ‘hinges’ are occurring and determine if they are characteristic to the non-helical or helical domains. Additionally, we can utilize the information known about the sequence of type I collagen helices and the mechanical properties of the molecules to match the ranges to specific amino acids.
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