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Folding of polyglutamine chains.

Manan Chopra¹, Allam S Reddy, N L Abbott

¹Department of Chemical Engineering, University of Wisconsin, Madison, Wisconsin 53706-1691, USA.

The Journal of Chemical Physics

|December 3, 2008

Summary

This summary is machine-generated.

The folding of polyglutamine (PolyQ) chains into beta-helical structures is crucial for neurodegenerative diseases like Huntington's. Simulations reveal key contacts initiate folding, forming a nucleus for amyloid fibril formation in PolyQ chains longer than 36 residues.

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Assays for the Degradation of Misfolded Proteins in Cells

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Area of Science:

Biophysics
Computational Biology
Neuroscience

Background:

Long polyglutamine (PolyQ) chains are implicated in neurodegenerative diseases.
Expanded PolyQ sequences (>36 residues) correlate with Huntington's disease onset.

Purpose of the Study:

Investigate the folding pathway of a 54-residue PolyQ chain into a beta-helical structure.
Understand the role of solvent models in PolyQ folding.
Identify critical factors for PolyQ chain folding and amyloid nucleus formation.

Main Methods:

Transition path sampling Monte Carlo simulations.
Simulations conducted in explicit water and implicit solvent models.
Analysis of folding pathways and critical contact formation.

Main Results:

The formation of a few critical contacts is necessary and sufficient for PolyQ chain folding.
Once critical contacts form, the chain is committed to folding.
A stable beta-helical structure can act as a nucleus for amyloid fibril polymerization.
PolyQ sequences shorter than 36 residues cannot form this nucleus.
Specific mutations can exacerbate the stability of the beta-helical structure.

Conclusions:

PolyQ chain folding is initiated by a small set of critical contacts.
The beta-helical structure serves as a critical nucleus for PolyQ aggregation.
The length threshold of 36 residues is significant for forming the amyloid nucleus.
Understanding PolyQ folding pathways offers insights into neurodegenerative disease mechanisms.