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Dimethylsulfoxide-quenched hydrogen/deuterium exchange method to study amyloid fibril structure.

Biochimica et biophysica acta (2007-05-15)
Masaru Hoshino, Hidenori Katou, Kei-ichi Yamaguchi, Yuji Goto
ABSTRACT

A general method to analyze the structure of a supramolecular complex of amyloid fibrils at amino acid residue resolution has been developed. This method combines the NMR-detected hydrogen/deuterium (H/D) exchange technique to detect hydrogen-bonded amide groups and the ability of the aprotic organic solvent dimethylsulfoxide (DMSO) to dissolve amyloid fibrils into NMR-observable, monomeric components while suppressing the undesired H/D exchange reaction. Moreover, this method can be generally applied to amyloid fibrils to elucidate the distribution of hydrogen-bonded amino acid residues in the three-dimensional molecular organization in the amyloid fibrils. In this study, we describe theoretical considerations in the H/D exchange method to obtain the structural information of proteins, and the DMSO-quenched H/D exchange method to study a supramolecular complex of amyloid fibrils. A possible application of this method to study the interaction of a protein/peptide with phospholipid membrane is also discussed.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Deuterium, 99.8 atom % D
Sigma-Aldrich
Deuterium, 99.96 atom % D
Sigma-Aldrich
Deuterium, 99.9 atom % D

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