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This work is devoted to the characterization of type I collagen treated by a low-temperature plasma jet generated in ambient air to determine whether the resulting fibrous material is structurally preserved or reinforced. The physical structure of collagen is checked by differential scanning calorimetry (DSC), which is a well suited technique to analyze thermal transitions in proteins, such as denaturation. DSC is used to evaluate the thermal stability of collagen after the plasma treatments while Fourier transform infra red spectroscopy is used to check the integrity of triple helical domain and to investigate the effects of plasma treatments on the functional groups of collagen. It is more particularly shown that the plasma treatment can stabilize the collagen structure without altering the triple helical structure. This observation is supported by 1) the shift observed toward high-temperature range of the collagen denaturation and 2) the stiffening of the chains by a cross-linking action when compared to the control sample.