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DOI: 10.3791/66275-v
Intrinsically disordered regions (IDRs) are flexible protein domains that modify their conformation in response to environmental changes. Ensemble fluorescence resonance energy transfer (FRET) can estimate protein dimensions under different conditions. We present a FRET approach to assess IDR structural sensitivity in living Saccharomyces cerevisiae cells under hyperosmotic stress.
We aim to understand how intrinsically disorder regions sense and respond to changes in the physical chemical properties of the environment. We combine biophysical, biochemical, genetic, and cell biology techniques to monitor how the structural ensemble of disorder regions change in living cells. Protein biophysics techniques are currently used to study the confirmation of IDRs.
These include nuclear magnetic resonance, circular dichroism, small angle x-ray scattering, and FRET. Most of these techniques can only be used in vitro. Studying the confirmation of IDRs in a cellular context is challenging with high cost and time consuming techniques.
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