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The von Willebrand Factor (vWF) is a large multimeric protein in the blood that aids in blood clotting. It activates the clotting cascade at specific time and specific place, which is one of the human body's masterpieces in targeted molecular manipulation. Hydrodynamic forces trigger conformational changes of vWF, by which its potency and reactivity are regulated. In this thesis, inspiration is taken from novel findings in vWF experiments. The present study aims to describe the behaviors in this process within the context of polymer science.

Using Brownian molecular dynamics simulations as well as Random Forest Algorithms, the internal dynamics and biomechanical response of von Willebrand Factor (vWF) multimers subject to shear flows are examined. The coarse-grained multimer description employed here is based on a monomer model in which the A2 domain of vWF is explicitly represented by a non-linear elastic spring whose mechanical response was fit to experimental force/extension data from vWF monomers.