Add like
Add dislike
Add to saved papers

Ultrafast Protein Folding in Membrane-Mimetic Environments.

Proteins fold on timescales from hours to microseconds. In addition to protein size, sequence, and topology, the environment represents an equally important factor in determining folding speed. This is particularly relevant for proteins that require a lipid membrane or a membrane mimic to fold. However, only little is known about how properties of such a hydrophilic/hydrophobic interface modulate the folding landscape of membrane-interacting proteins. Here, we studied the influence of different membrane-mimetic micellar environments on the folding and unfolding kinetics of the helical-bundle protein Mistic. Devising a single-molecule fluorescence spectroscopy approach, we extracted folding and unfolding rates under equilibrium conditions and dissected the contributions from different detergent moieties to the free-energy landscape. While both polar and nonpolar moieties contribute to stability, they exert differential effects on the free-energy barrier: Hydrophobic burial stabilizes the folded state but not the transition state in reference to a purely aqueous environment; by contrast, zwitterionic headgroup moieties stabilize the folded state and, additionally, lower the free-energy barrier to accelerate the folding of Mistic to achieve ultrafast folding times down to 35μs.

Full text links

We have located links that may give you full text access.
Can't access the paper?
Try logging in through your university/institutional subscription. For a smoother one-click institutional access experience, please use our mobile app.

For the best experience, use the Read mobile app

Mobile app image

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app

All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.

By using this service, you agree to our terms of use and privacy policy.

Your Privacy Choices Toggle icon

You can now claim free CME credits for this literature searchClaim now

Get seemless 1-tap access through your institution/university

For the best experience, use the Read mobile app