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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 J+Am+Soc+Mass+Spectrom
2016 ; 27
(3
): 451-61
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Ion Mobility Spectrometry-Hydrogen Deuterium Exchange Mass Spectrometry of
Anions: Part 2 Assessing Charge Site Location and Isotope Scrambling
#MMPMID26802030
J Am Soc Mass Spectrom
2016[Mar]; 27
(3
): 451-61
PMID26802030
show ga
Ion mobility spectrometry (IMS) coupled with gas-phase hydrogen deuterium
exchange (HDX)-mass spectrometry (MS) and molecular dynamic simulations (MDS) has
been used for structural investigation of anions produced by electrospraying a
sample containing a synthetic peptide having the sequence KKDDDDDIIKIIK. In these
experiments the potential of the analytical method for locating charge sites on
ions as well as for utilizing collision-induced dissociation (CID) to reveal the
degree of deuterium uptake within specific amino acid residues has been assessed.
For diffuse (i.e., more elongated) [M - 2H](2-) ions, decreased deuterium content
along with MDS data suggest that the D4 and D6 residues are charge sites, whereas
for the more diffuse [M - 3H](3-) ions, the data suggest that the D4, D7, and the
C-terminus are deprotonated. Fragmentation of mobility-selected, diffuse [M -
2H](2-) ions to determine deuterium uptake at individual amino acid residues
reveals a degree of deuterium retention at incorporation sites. Although the
diffuse [M - 3H](3-) ions may show more HD scrambling, it is not possible to
clearly distinguish HD scrambling from the expected deuterium uptake based on a
hydrogen accessibility model. The capability of the IMS-HDX-MS/MS approach to
provide relevant details about ion structure is discussed. Additionally, the
ability to extend the approach for locating protonation sites on
positively-charged ions is presented.