Unknown

Dataset Information

0

Multiple gas-phase conformations of proline-containing peptides: is it always cis/trans isomerization?


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.

SUBMITTER: Lietz CB 

PROVIDER: S-EPMC4972606 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Multiple gas-phase conformations of proline-containing peptides: is it always cis/trans isomerization?

Lietz Christopher B CB   Chen Zhengwei Z   Yun Son Chang C   Pang Xueqin X   Cui Qiang Q   Li Lingjun L  

The Analyst 20160801 16


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.  ...[more]

Similar Datasets

| S-EPMC2566824 | biostudies-literature
| S-EPMC3624761 | biostudies-literature
| S-EPMC2143535 | biostudies-other
| S-EPMC5708682 | biostudies-literature
| S-EPMC11291072 | biostudies-literature
| S-EPMC9237829 | biostudies-literature
| S-EPMC3864314 | biostudies-literature
| S-EPMC4077359 | biostudies-literature
| S-EPMC2590911 | biostudies-literature
| S-EPMC6166725 | biostudies-literature