Stress-induced molecular rearrangement in tendon collagen.

Tension-induced molecular rearrangements in wet native fibres of rat-tail tendons and human finger flexor tendons are registered with the help of time-resolved diffraction spectra using synchrotron radiation. The tension-induced increase of the 67 nm D period is combined with changes in the intensities of some orders of the meridional small angle reflection. Both effects are reversible when unloading the fibre, but are preserved when the load is held constant until the fibre tears. The increase in the D period is partly due to a sliding of the triple helices relative to each other and partly due to a stretching of the triple helices themselves. The sliding of the triple helices results in an alteration of the D stagger, leading to a change in the length of the gap and overlap regions, and to a stretching of the cross-linked telopeptides. This interpretation is supported by comparison with the relative intensities derived from a model with varying length of gap and overlap regions, as well as by comparison with model calculations that include the telopeptides.