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- Title
Diversity in Gold Finger Structure Elucidated by Traveling-Wave Ion Mobility Mass Spectrometry.
- Authors
Du, Zhifeng; de Paiva, Raphael E. F.; Nelson, Kristina; Farrell, Nicholas P.
- 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 AuI metallopeptide ions that were formed by ZnII 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.
- Subjects
ION mobility; MASS spectrometry; PROTEIN analysis; PEPTIDE analysis; ZINC-finger proteins; TRANSCRIPTION factor Sp1
- Publication
Angewandte Chemie, 2017, Vol 129, Issue 16, p4535
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201612494