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Updated: Jun 25, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

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Stabilizing Effect of Neighboring Disordered RGG Domain on the Folded State of FUS-RRM.

Kosar Rahimi¹, Ayush Gupta¹, Karim Malekzadeh¹

¹Department of Chemical and Biomolecular Engineering, University of Houston, Houston, Texas 77204, United States.

The Journal of Physical Chemistry. B

|June 23, 2026

Summary

The disordered RGG region stabilizes the folded RNA-recognition motif (RRM) of FUS protein by forming contacts that wrap around it. This interaction is crucial for maintaining RRM stability and preventing misfolding linked to neurodegenerative diseases.

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Published on: January 12, 2024

Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Fused in Sarcoma (FUS) protein is vital for RNA processing.
Its RNA-recognition motif (RRM) can unfold and aggregate, contributing to amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD).
The effect of adjacent sequences on FUS RRM stability is not well understood.

Purpose of the Study:

To investigate how the flanking RGG sequence influences the stability of the FUS RRM.
To characterize the folding landscape of FUS RRM using advanced simulation techniques.
To understand the molecular mechanisms of disordered-ordered interdomain interactions in FUS.

Main Methods:

Atomistic molecular dynamics simulations were performed.
Rare-event sampling was achieved using multithermal-multiumbrella on-the-fly probability enhanced sampling (MM-OPES).
Simulations were conducted on isolated FUS RRM and FUS RRM with the adjacent RGG sequence.

Main Results:

The disordered RGG segment significantly enhances the stability of the folded FUS RRM.
Stabilization occurs through intramolecular contacts where the RGG segment wraps around the RRM domain.
Specific interactions involve increased α1 helix, β2, β3 strands, and the KK loop, mediated by RGG-RRM residue contacts.

Conclusions:

Disordered regions can stabilize folded domains through specific interdomain contacts.
The RGG region's interaction with FUS RRM is critical for maintaining its structural integrity.
Disruption of these interactions may lead to RRM destabilization and contribute to FUS-related proteinopathies.