Abstract
The effect of conformational fluctuations of modular macromolecules, such as enzymes, on their diffusion properties is addressed using a simple generic model of an asymmetric dumbbell made of two hydrodynamically coupled subunits. It is shown that equilibrium fluctuations can lead to an interplay between the internal and the external degrees of freedom and give rise to negative contributions to the overall diffusion coefficient. Considering that this model enzyme explores a mechanochemical cycle, we show how substrate binding and unbinding affects its internal fluctuations, and how this can result in an enhancement of the overall diffusion coefficient of the molecule. These theoretical predictions are successfully confronted with recent measurements of enzyme diffusion in dilute conditions using fluorescence correlation spectroscopy.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
