Abstract
The composition of solutes in the cell routinely fluctuates due to external stress or cell cycle progression. While many proteins may be resilient to these fluctuations, intrinsically disordered protein regions, or IDRs, can be sensitive to changes in their surrounding solution. This is due to a low content of intramolecular bonds and high surface area exposed to their surrounding environment. However, the molecular grammar that dictates this sensitivity in IDRs remains poorly understood. In this project we use Förster Resonance Energy Transfer (FRET) paired with live cell microscopy to characterize the ensemble of a library of synthetic IDR in cells under stressed conditions.
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.
