Solution

ID: past-exam-of-the-biological-physics-course-of-the-university-of-oxford/2015/4/c/solution

An inextensible worm-like chain describes entropic elasticity and diverges as . Real protein backbones and folded protein domains also deform energetically under large forces. For an axial stretch modulus , a simple extensible-chain correction is
The last term supplies extension through bond and structural deformation that the inextensible model excludes. It becomes especially noticeable on the high-force ends of rising branches.[ref] An unfolding transition itself is also outside a single equilibrium fixed- branch. These mechanisms explain why the source explicitly distinguishes energetic and entropic elasticity.
Source-dependent TODO: the arrows and actual deviations at the first four peaks in Figure B are unavailable. Energetic stretching is the natural explanation of a high-force excess-extension deviation, but its direction, onset, and uniqueness cannot be checked against the missing curves. No particular arrow-marked feature or numerical stretch modulus is invented. This source-dependent identification remains incomplete; the recoverable model limitation is explained above.

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