Fig. 4 | Nature Communications

Fig. 4

From: Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity

Fig. 4

Disulfide bonds decrease the mechanical stability of titin Ig domains. a Typical unfolding traces of (I69)8 recorded with a linear force increase of 40 pN s−1. Blue asterisks mark the unfolding events of I69reduced (26 nm steps in the blue upper trace) whereas red asterisks correspond to unfolding steps of I69oxidized (6 nm steps in the red lower trace). Isomerization reactions are detected as additional steps (gray triangles). b Unfolding forces and step sizes are represented in a bidimensional histogram. Average values appear as white crosses

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