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. Author manuscript; available in PMC: 2016 May 1.
Published in final edited form as: Biochem Biophys Res Commun. 2015 Mar 18;460(2):434–438. doi: 10.1016/j.bbrc.2015.03.051

Figure 4. Altering the parameters of the entropic elasticity affects protein folding.

Figure 4

A) Decreasing the contour length of our polyprotein from ΔLc = 38 nm to ΔLc = 9.5 nm, shifts the global minimum free energy from favoring the completely unfolded state to the completely folded state at a constant force of F =12 pN. Hence, the rate of folding is considerably increased by the decreasing ΔLc. B) A similar effect is captured by altering the persistence length at a constant force of F = 12 pN. Increasing the stiffness of the polymer from p = 0.2 nm to p = 0.7 nm also shifts the minimum free energy from fully folded to fully unfolded.