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Related Experiment Video

Updated: Jul 10, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

Sequence-ensemble-function relationships for disordered proteins in live cells.

Alex Holehouse¹, Ryan Emenecker, Karina Guadalupe²

¹Washington University in St. Louis.

Research Square

|November 21, 2023

Summary

This summary is machine-generated.

Intrinsically disordered protein regions (IDRs) link sequence to cellular function. We designed synthetic IDRs and found their structure and function, like sensing cell volume changes, depend on their amino acid sequence.

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Last Updated: Jul 10, 2025

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

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Published on: January 5, 2024

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Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses

Published on: January 12, 2024

Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

Intrinsically disordered protein regions (IDRs) are crucial for cellular processes.
IDRs adopt diverse structures (an ensemble) dictated by their amino acid sequence.
The precise relationship between IDR sequence, ensemble properties, and cellular function remains unclear.

Conclusions:

Established a clear connection between IDR sequence, ensemble, and function in a cellular context.
Enabled the design of synthetic IDRs with de novo functions, such as volume sensing.
Provided a foundation for understanding IDR sequence-function relationships and designing novel IDR-based tools.