Premium
Diversity in Gold Finger Structure Elucidated by Traveling‐Wave Ion Mobility Mass Spectrometry
Author(s) -
Du Zhifeng,
de Paiva Raphael E. F.,
Nelson Kristina,
Farrell Nicholas P.
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201612494
Subject(s) - zinc finger , ion mobility spectrometry , chemistry , peptide , mass spectrometry , zinc , conformational isomerism , ion , crystallography , biophysics , transcription factor , stereochemistry , molecule , biochemistry , biology , chromatography , organic chemistry , gene
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.