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. Author manuscript; available in PMC: 2020 Jan 10.
Published in final edited form as: J Phys Chem B. 2018 Dec 31;123(1):21–28. doi: 10.1021/acs.jpcb.8b07501

Figure 7.

Figure 7.

Equation 15 shows that the strain parameters r, β, and ξ decay exponentially while oscillating with the periodicity of the double helix. Let us assume that the protein binding at x = 0 increases the radius of the double helix from a to a + r0. This change in radius at x = 0 decays exponentially while oscillating with the periodicity of the double helix, away from the binding site. Similar behavior is observed for other strain parameters, β and ξ. Due to this sinusoidal modulation of the geometry, the binding of the second protein is facilitated at some locations, while inhibited at others; this manifests as an exponentially decaying oscillatory behavior observed in the allosteric interaction energy (ΔG).