Issue 73, 2018

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

Abstract

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

Supplementary files

Article information

Article type
Communication
Submitted
09 Jun 2018
Accepted
25 Jul 2018
First published
25 Jul 2018

Chem. Commun., 2018,54, 10248-10251

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

J. Froberg, W. Choi, A. Sedigh, T. Anajafi, J. Farmakes, Z. Yang, S. Mallik, D. K. Srivastava and Y. Choi, Chem. Commun., 2018, 54, 10248 DOI: 10.1039/C8CC04601H

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements