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Abstract | Cited by

The dynamic interactions of an individual matrix metalloproteinase-1 were imaged and monitored in the presence of either triple-helical or non-triple-helical, partially structured collagen-mimic substrates. The enzyme exhibited ten-fold increased catalytic turnover rates with the structurally modified substrate by skipping the triple-helix unwinding step during the catalytic pathway.

Graphical abstract: Real-time tracking of single-molecule collagenase on native collagen and partially structured collagen-mimic substrates

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