4.8 Article

Processive enzyme mimic: Kinetics and thermodynamics of the threading and sliding process

Publisher

NATL ACAD SCIENCES
DOI: 10.1073/pnas.0603036103

Keywords

biomimetic; physical organic; rotaxanes; supramolecular chemistry

Ask authors/readers for more resources

The kinetics and thermodynamics of the treading and dethreading process of polymers through the cavity of a synthetic toroidal host is investigated by studying its complexation with a series of end-functionalized polymers of different lengths containing an end group that is selectively recognized by the host. The system is designed in such a way that complexation is only observed if the host has traveled all of the way across the complete polymer. Detailed kinetic investigations using fluorescence spectroscopy have revealed that the barrier for this process is length dependent and most likely related to the stretching of the polymer. Moreover, the results indicate that our previously reported processive enzyme mimic most likely operates by randomly sliding along its macromolecular substrate.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available