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. Author manuscript; available in PMC: 2016 Mar 20.
Published in final edited form as: J Am Chem Soc. 2012 Aug 1;134(32):13259–13265. doi: 10.1021/ja212170b

Figure 5.

Figure 5

Energetic landscape for collagen proteolysis by MMP-1. (a) The heterotrimeric MMP-1 binding site is partially unwound even in the absence of applied load. Approximately 6 times the thermal energy (6 kBT) separates the MC and MC* states (black; see text). A 0.57 nm increase in length accompanies the transition from MC to MC*. 15 pN external load stabilizes MC* by 8.6 pN·nm, or ~2 kBT (red). (b) Approximately 8 kBT separate MC and MC* for the homotrimeric MMP-1 recognition site (black; see text). A 1.4 nm length increase accompanies the transition to the stretched state, resulting in ~5 kBT stabilization of MC* at 15 pN of load (red).