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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6145137 | PMC |
| http://dx.doi.org/10.1039/c8cc04601h | DOI Listing |
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