Multiple gas-phase conformations of proline-containing peptides: is it always cis/trans isomerization?
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SCOPUS
- Title
- Multiple gas-phase conformations of proline-containing peptides: is it always cis/trans isomerization?
- Authors
- SON, CHANG YUN; Lietz, Christopher B.; Chen, Zhengwei; Pang, Xueqin; Cui, Qiang; Li, Lingjun
- Date Issued
- 2016-07
- Publisher
- Royal Society of Chemistry
- Abstract
- Ion mobility-mass spectrometry (IM-MS) is often employed to look at the secondary, tertiary, and quaternary structures of naked peptides and proteins in the gas-phase. Recently, it has offered a unique glimpse into proline-containing peptides and their cis/trans Xxx-Pro isomers. An experimental "signature" has been identified wherein a proline-containing peptide has its Pro residues substituted with another amino acid and the presence or absence of conformations in the IM-MS spectra is observed. Despite the high probability that one could attribute these conformations to cis/trans isomers, it is also possible that cis/trans isomers are not the cause of the additional conformations in proline-containing peptides. However, the experimental evidence of such a system has not been demonstrated or reported. Herein, we present the IM-MS analysis of Neuropeptide Y's wild-type (WT) signal sequence and Leu7Pro (L7P) mutant. Although comparison of arrival times and collision cross-sections of [M + 4H](4+) ions yields the cis/trans "signature", molecular dynamics indicates that a cis-Pro7 is not very stable and that trans-Pro7 conformations of the same cross-section arise with equal frequency. We believe that this work further underscores the importance of theoretical calculations in IM-MS structural assignments.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/103381
- DOI
- 10.1039/C5AN00835B
- ISSN
- 0003-2654
- Article Type
- Article
- Citation
- Analyst, vol. 141, no. 16, page. 4863 - 4869, 2016-07
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