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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

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Conformational properties of beta-PrP.

Laszlo L P Hosszu¹, Clare R Trevitt², Samantha Jones²

¹MRC Prion Unit, Department of Neurodegenerative Disease, Institute of Neurology, Queen Square, London WC1N 3BG; Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN.

The Journal of Biological Chemistry

|April 17, 2009

Summary

Prion protein (PrPC) transforms into a beta-sheet-rich form (PrPSc), inhibiting proteasomes. This study reveals acidic conditions induce oligomerization of a PrP fragment, highlighting early conformational changes in prion disease.

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A Protocol for Computer-Based Protein Structure and Function Prediction

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Published on: November 3, 2011

Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Prion diseases involve the misfolding of cellular prion protein (PrPC) into a beta-sheet-rich isoform (PrPSc).
Understanding this conformational transition is key to elucidating prion disease mechanisms.

Purpose of the Study:

To investigate the conformational properties of a disulfide-reduced human prion protein fragment (residues 91-231) under acidic conditions.
To characterize the structural intermediates and oligomeric states involved in the transition towards a beta-sheet-rich conformation.

Main Methods:

Heteronuclear Nuclear Magnetic Resonance (NMR) spectroscopy
Analytical ultracentrifugation
Circular Dichroism (CD) spectroscopy

Main Results:

Under acidic conditions, the PrP fragment forms soluble oligomers with significant beta-sheet content, similar to PrPSc.
The monomeric precursor resembles a molten globule intermediate, retaining some helical structure (helices I and III) but lacking helical structure in helix II.
This intermediate is compact, and upon oligomerization, residues 126-227 become immobilized, while other regions remain mobile.

Conclusions:

The study identifies a molten globule-like intermediate in the acid-induced conversion of PrP, pinpointing helix II as a key interaction site.
These findings provide insights into the early molecular events driving the conformational changes associated with prion diseases.
The oligomeric form exhibits potent inhibition of the 26S proteasome, suggesting a link between structural changes and functional impairment.