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First atomic-level look at a protein that causes brain disease
Date:4/22/2008

brils are very large and complex, and so traditional biochemical techniques wont reveal their structure in detail, Jaroniec said.

The assistant professor of chemistry at Ohio State is an expert in a technique that can reveal the structure of such large molecules: solid-state nuclear magnetic resonance (NMR) spectroscopy.

NMR works by tuning into the radio waves emitted by atoms within materials. Every atom emits radio waves at a particular frequency, depending on the types of atoms that surround it.

The NMR technique the chemists used, called magic angle spinning, involves spinning materials at a certain angle with respect to the NMR's magnetic field in order to remove radio interference among the atoms. It offers researchers a clear view of which atoms make up a particular molecule, and how those atoms are arranged.

So after the researchers let the prion proteins fold into amyloid fibrils, they used magic angle spinning NMR to study the fibrils structure.

They searched the NMR signals for the chemical tags that had been planted in the prions. In that way, they were able to determine what parts of the original prion protein were contained within the fibrils.

They found, to their surprise, that some 80 percent of the original prion protein molecule was not present in the fibrils. The fibrils consisted exclusively of the remaining 20 percent -- approximately 29 amino acids, of which two appear to be especially critical to the structure of the molecule.

Other studies have suggested that these two amino acids, numbered 138 and 139, were key to the formation of the CAA fibrils, Jaroniec said. But this study is the first to confirm their importance by studying them at the atomic level.

The researchers are continuing this work, and plan to examine the structure of the fibrils in more detail, as well as other strains of the CAA prion protein.


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Contact: Christopher Jaroniec
jaroniec.1@osu.edu
614-247-4284
Ohio State University
Source:Eurekalert

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