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Diversity in Gold Finger Structure Elucidated by Traveling-Wave Ion Mobility Mass Spectrometry.

Diversity in Gold Finger Structure Elucidated by Traveling-Wave Ion Mobility Mass Spectrometry.
Author Information (click to view)

Du Z, de Paiva RE, Nelson K, Farrell NP,


Du Z, de Paiva RE, Nelson K, Farrell NP, (click to view)

Du Z, de Paiva RE, Nelson K, Farrell NP,

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Angewandte Chemie (International ed. in English) 2017 03 20() doi 10.1002/anie.201612494

Abstract

Traveling wave ion mobility (TWIM) mass spectrometry (MS) is a powerful method for the structural and conformational analysis of proteins and peptides, enabling the differentiation of isomeric peptides (or proteins) that have the same sequence but are modified at different residues. In this study, the TWIM-MS technique was used to separate isomeric Au(I) metallopeptide ions that were formed by Zn(II) displacement from the parent zinc fingers (ZFs). The synthetic gold finger peptides were derived from the C-terminus of the HIV nucleocapsid p7 protein (NCp7-F2) and finger 3 of the Sp1 transcription factor (Sp1-F3). TWIM-MS enabled the acquisition of distinct product ion spectra for each isomer, clearly indicating the binding sites for the major conformers in the presence of multiple coordination possibilities. Collision cross-section measurements showed that the aurated peptide has a slightly more compact structure than the parent zinc compound NCp7-F2, which showed only one conformation.

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