 Another example is found in protein folding within molecular biology (Hüttemann and Love 2011, Love and Hüttemann 2011). Functional proteins are folded structures composed of amino acid components linked together into a linear chain. If we ask whether the folded protein is mereologically composed of its amino acid parts given current representations in molecular biology, then the affirmative answer seems to favor explanatory reduction with respect to the spatial hierarchy. But if we ask whether the linear amino acid chain folds into a functional protein (a causal process with a temporal dimension) purely as consequence of its linked amino acid parts, then the answer is less clear. Empirical studies have discerned a necessary role for other folded proteins to assist in the proper folding of newly generated linear amino acid chains (Frydman 2001). That the linked amino acid components alone are insufficient causally, even if they are sufficient constitutionally, allows for a more explicit appreciation of the significance of temporality and dynamics (Mitchell 2009), especially because the relations of interest concern only molecular biological phenomena (as opposed to higher levels of organization, such as cells or anatomy).