H/D exchange of gas phase bradykinin ions in a linear quadrupole ion trap

Mao, Dunmin; Douglas, D. J.

doi:10.1016/s1044-0305(02)00818-8

Cited by 48 publications

(46 citation statements)

References 49 publications

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“…The maximum number of exchanges observed at this timescale and reagent pressure is 14. Although the H/D exchange of bradykinin with deuterated methanol has been previously reported, [12,20,22,24] the data are shown here to demonstrate the distribution of the labeled ion populations used in the fragmentation studies discussed below. Fig.…”

Section: H/d Exchange Of Doubly-protonated Bradykininmentioning

confidence: 52%

“…The ion mobility and H/D exchange of the nonapeptide bradykinin and related analogues have been extensively studied [10,12,[15][16][17][18][19][20][21][22][23][24][25][26][27][28]. Ion mobility measurements have shown that the singly-and doubly-protonated ions of bradykinin have a similar cross-section, while the triplyprotonated ion has a cross-section that is approximately 15% larger, providing evidence for a much less compact structure [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

“…Ion mobility measurements have shown that the singly-and doubly-protonated ions of bradykinin have a similar cross-section, while the triplyprotonated ion has a cross-section that is approximately 15% larger, providing evidence for a much less compact structure [15][16][17]. H/D exchange studies with D 2 O, CD 3 OD, ND 3 , and DI have detected two non-interconverting ion populations for doubly-and triply-protonated bradykinin [20,22,[24][25][26][27]. These ion populations were not detected by traditional ion mobility experiments [15][16][17], suggesting the conformers have a similar collisional cross-section.…”

Section: Introductionmentioning

confidence: 99%

“…In fact, scrambling of "mobile" protons and deuteriums in peptides is well-documented in the literature [31][32][33][34]. Mao and Douglas performed H/D exchange of bradykinin fragment ions y 6 , y 7 , y 8 , y 8 2+ , b 5 , a 6 , b 6 , and a 8 and observed that the y-ions exchange more readily [22]. They conclude this is consistent with the higher exchange level observed for singly-protonated des-arg 1 -bradykinin over singly-protonated des-arg 9 -bradykinin [22].…”

Section: Introductionmentioning

confidence: 99%

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Fragmentation of doubly-protonated peptide ion populations labeled by H/D exchange with CD3OD

Herrmann

Kuppannan

Wysocki

2006

International Journal of Mass Spectrometry

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Doubly-protonated bradykinin (RPPGFSPFR) and an angiotensin III analogue (RVYIFPF) were subjected to hydrogen/deuterium (H/D) exchange with CD 3 OD in a Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer. A bimodal distribution of deuterium incorporation was present for bradykinin after H/D exchange for 90 s at a CD 3 OD pressure of 4 × 10 −7 Torr, indicating the existence of at least two distinct populations. Bradykinin ion populations corresponding to 0-2 and 5-11 deuteriums (i.e., D 0 , D 1 , D 2 , D 5 , D 6 , D 7 , D 8 , D 9 , D 10 , and D 11 ) were each monoisotopically selected and fragmented via sustained off-resonance irradiation (SORI) collision-induced dissociation (CID). The D 0 -D 2 ion populations, which correspond to the slower exchanging population, consistently require lower SORI amplitude to achieve a similar precursor ion survival yield as the faster-reacting (D 5 -D 11 ) populations. These results demonstrate that conformation/ protonation motif has an effect on fragmentation efficiency for bradykinin. Also, the partitioning of the deuterium atoms into fragment ions suggests that the C-terminal arginine residue exchanges more rapidly than the N-terminal arginine. Total deuterium incorporation in the b 1 /y 8 and b 2 /y 7 ion pairs matches very closely the theoretical values for all ion populations studied, indicating that the ions of a complementary pair are likely formed during the same fragmentation event, or that no scrambling occurs upon SORI. Deuterium incorporation into the y 1 /a 8 pseudo-ion pair does not closely match the expected theoretical values. The other peptide, doubly-protonated RVYIFPF, has a trimodal distribution of deuterium incorporation upon H/D exchange with CD 3 OD at a pressure of 1 × 10 −7 Torr for 600 s, indicating at least three distinct ion populations. After 90 s of H/D exchange where at least two distinct populations are detected, the D 0 -D 7 ion populations were monoisotopically selected and fragmented via SORI-CID over a range of SORI amplitudes. The precursor ion survival yield as a function of SORI amplitude falls into two distinct behaviors corresponding to slower-and faster-reacting ion populations. The slower-reacting population requires larger SORI amplitudes to achieve the same precursor ion survival yield as the faster exchanging population. Total deuterium incorporation into the y 2 /b 5 ion pairs matches closely the theoretical values over all ion populations and SORI amplitudes studied. This result indicates the y 2 and b 5 ions are likely formed by the same mechanism over the SORI amplitudes studied.

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Section: H/d Exchange Of Doubly-protonated Bradykininmentioning

confidence: 52%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Fragmentation of doubly-protonated peptide ion populations labeled by H/D exchange with CD3OD

Herrmann

Kuppannan

Wysocki

2006

International Journal of Mass Spectrometry

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“…In contrast, mass spectrometry requires little sample, and with electrospray ionization (ESI) or soft laser desorption/ionization (John Fenn and Kiochi Tanaka 2002 in chemistry), a wide variety of biomolecules and specific complexes can be introduced into a mass spectrometer. A number of methods have been developed to probe the general three-dimensional shapes of biomolecule ions and noncovalent complexes using the techniques of ion mobility [1][2][3][4][5][6][7][8], H/D exchange both in solution [9,10] and the gas phase [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28], and proton-transfer reactivity [29,30].…”

mentioning

confidence: 99%

Further studies on the origins of asymmetric charge partitioning in protein homodimers

Jurchen

García

Williams

2004

J. Am. Soc. Mass Spectrom.

115

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Dissociation of gas-phase protonated protein dimers into their constituent monomers can result in either symmetric or asymmetric charge partitioning. Dissociation of ␣-lactalbumin homodimers with 15ϩ charges results in a symmetric, but broad, distribution of protein monomers with charge states centered around 8ϩ/7ϩ. In contrast, dissociation of the 15ϩ heterodimer consisting of one molecule in the oxidized form and one in the reduced form results in highly asymmetric charge partitioning in which the reduced species carries away predominantly 11ϩ charges, and the oxidized molecule carries away 4ϩ charges. This result cannot be adequately explained by differential charging occurring either in solution or in the electrospray process, but appears to be best explained by the reduced species unfolding upon activation in the gas phase with subsequent separation and proton transfer to the unfolding species in the dissociation complex to minimize Coulomb repulsion. For dimers of cytochrome c formed directly from solution, the 17ϩ charge state undergoes symmetric charge partitioning whereas dissociation of the 13ϩ is asymmetric. Reduction of the charge state of dimers with 17ϩ charges to 13ϩ via gas-phase proton transfer and subsequent dissociation of the mass selected 13ϩ ions results in a symmetric charge partitioning. This result clearly shows that the structure of the dimer ions with 13ϩ charges depends on the method of ion formation and that the structural difference is responsible for the symmetric versus asymmetric charge partitioning observed. This indicates that the asymmetry observed when these ions are formed directly from solution must come about due either to differences in the monomer conformations in the dimer that exist in solution or that occur during the electrospray ionization process. These results provide additional evidence for the origin of charge asymmetry that occurs in the dissociation of multiply charged protein complexes and indicate that some solution-phase information can be obtained from these gas-phase dissociation experiments. (J Am Soc Mass

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Conformational changes of ubiquitin during electrospray ionization as determined by in‐ESI source H/D exchange combined with high‐resolution MS and ECD fragmentation

et al. 2014

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In the paper, we have demonstrated the possibility of performing hydrogen/deuterium (H/D) exchange of proteins in the region of gas-phase ion formation in an electrospray ion source by saturating the electrospray ionization source with vapors of a deuterating agent (D(2)O or MeOD). In this region, charged droplets are shrinking and the protein ions transfer into the gas phase. As a model protein, we have used ubiquitin whose ion mobility spectrometry and gas-phase H/D exchange in the vacuum part of a mass spectrometer demonstrated the presence of gas-phase conformers with different cross sections and H/D exchange rates. In our experiments, we observed monomodal deuterium distributions for all solvents, charge states, desolvating capillary temperature and types of deuterating agent. Also, we found that the number of H/D exchanges increases with an increasing desolvating capillary temperature and decreasing charge state. We observed that solution composition (49 : 50 : 1 H(2)O : MeOH : formic acid or 99 : 1 H(2)O : formic acid) influences the charge-state distribution but did not change the degree of H/D exchange for the same charge state. Electron-capture dissociation fragmentation shows that higher charge states contain a segment that is protected from access by the deuterating agent.

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H/D exchange of gas phase bradykinin ions in a linear quadrupole ion trap

Cited by 48 publications

References 49 publications

Fragmentation of doubly-protonated peptide ion populations labeled by H/D exchange with CD3OD

Fragmentation of doubly-protonated peptide ion populations labeled by H/D exchange with CD3OD

Further studies on the origins of asymmetric charge partitioning in protein homodimers

Conformational changes of ubiquitin during electrospray ionization as determined by in‐ESI source H/D exchange combined with high‐resolution MS and ECD fragmentation

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