ライフサイエンスコーパス: IRMPD

1 IRMPD can offer advantages over collision-induced dissoc

2 IRMPD experiments were performed on milk oligosaccharide

3 IRMPD is also used for multiadduct dissociation in order

4 IRMPD of peptide cations allowed the detection of low m/

5 IRMPD of these cross-linked peptides resulted in seconda

6 IRMPD provided abundant fragment ions, primarily through

7 IRMPD should also be more easily paired with fluctuating

8 IRMPD spectroscopy combined with computational modeling

9 IRMPD spectroscopy is clearly not a proteomics tool.

10 IRMPD spectroscopy, which takes advantage of the high se

11 IRMPD yielded comparable information to previously repor

12 IRMPD, on the other hand, is independent of the value of

13 ations in resonant frequencies do not affect IRMPD.

14 Thermal assistance allows IRMPD to be used at or near optimal pressures, which res

15 Also, IRMPD showed an increased selectivity toward backbone cl

16 as applied for the interpretation of CAD and IRMPD MS/MS spectra collected for seven unmodified pepti

17 CAD and IRMPD of Ag-adducted phospholipids with unsaturated fatt

18 wo major characteristics distinguish CAD and IRMPD spectra for a given parent ion.

19 on efficiency is lower than those of CAD and IRMPD.

20 tigated the efficiency of ECD versus CID and IRMPD for top-down MS/MS analysis of multiply charged in

21 CID and IRMPD produced more cleavages in the vicinity of the sit

22 CID and IRMPD spectra of several oligosaccharides were also comp

23 on, were similarly presented in both CID and IRMPD spectra.

24 g glucosamine cleavages, compared to CID and IRMPD, because of high energy, single-photon absorption,

25 the collision-induced dissociation (CID) and IRMPD spectra of oligosaccharide alditols revealed that

26 tic digest of cytochrome c with both ECD and IRMPD as fragmentation modes.

27 orm, permitting implementation of AI-ETD and IRMPD on commercial mass spectrometers and broadening th

28 n fully characterized by CID experiments and IRMPD spectroscopy.

29 a highly convergent approach, and IM-MS and IRMPD-MS data were second collected.

30 of larger proteins (approximately 29 kDa) as IRMPD substantially improved protein identification and

31 Striking differences between IRMPD in the low pressure cell and CID in the high press

32 nd peptides which have been characterized by IRMPD spectroscopy, specific signatures of PTMs such as

33 ia electrospray ionization (ESI) followed by IRMPD of the resulting product ion complex produces sele

34 The fragment ions obtained by IRMPD are similar to those obtained by CAD and allow fac

35 Our results show that CAD, IRMPD, and EID provide complementary structural informat

36 kimmer dissociation and conventional in-cell IRMPD reveals a significant improvement in signal-to-noi

37 ast to collision-induced dissociation (CID), IRMPD offered the ability to selectively differentiate p

38 sive fragmentation of large peptides by CID, IRMPD, and particularly ECD, in conjunction with the hig

39 Unlike CID, IRMPD allows small product ions, those less than about o

40 collisional (Q-ToF and FT-ICR) or continuous IRMPD activation (FT-ICR).

41 ) followed by mild collisional or continuous IRMPD activation, resulting in a spectrum in which the c

42 In contrast, IRMPD and EID have had very limited, if any, application

43 f polymers using infrared multiphoton decay (IRMPD) and electron capture dissociation (ECD) as fragme

44 This selective DIA IRMPD LC/MS-based approach allows identification and ann

45 mode with infrared multiphoton dissociation (IRMPD) accompanied by improved phosphopeptide sensitivit

46 h a short infrared multiphoton dissociation (IRMPD) activation in the low-pressure cell.

47 er CID or infrared multiphoton dissociation (IRMPD) alone.

48 on (CID), infrared multiphoton dissociation (IRMPD) and electron capture dissociation (ECD); however,

49 MS) using infrared multiphoton dissociation (IRMPD) and electron-induced dissociation (EID) have prev

50 employed, infrared multiphoton dissociation (IRMPD) and electron-induced dissociation (EID), with 2DM

51 including infrared multiphoton dissociation (IRMPD) and electron-induced dissociation (EID).

52 zed using infrared multiphoton dissociation (IRMPD) and nano-liquid chromatography/mass spectrometry

53 on (AI-ETD) and IR multiphoton dissociation (IRMPD) experiments can be carried out as effectively as

54 (CAD) and infrared multiphoton dissociation (IRMPD) experiments were used to determine the site of ox

55 erforming infrared multiphoton dissociation (IRMPD) external to the mass analyzer in an external ion

56 10.6-mum infrared multiphoton dissociation (IRMPD) for the characterization of lipid A structures wa

57 s, LC ESI infrared multiphoton dissociation (IRMPD) FT-ICR MS yields mostly b and y fragment ions for

58 Infrared multiphoton dissociation (IRMPD) has been used in mass spectrometry to fragment pe

59 ciency of infrared multiphoton dissociation (IRMPD) in a quadrupole ion trap (QIT) is described.

60 Infrared multiphoton dissociation (IRMPD) in a quadrupole ion trap coupled to high-performa

61 to permit infrared multiphoton dissociation (IRMPD) in each of the two cells-the first a high pressur

62 o perform infrared multiphoton dissociation (IRMPD) in the low-pressure trap of a dual-cell quadrupol

63 erforming infrared multiphoton dissociation (IRMPD) is presented in which a hollow fiber waveguide (H

64 I-ECD) or infrared multiphoton dissociation (IRMPD) mass spectrometry techniques to overcome these re

65 rmined by infrared multiphoton dissociation (IRMPD) MS(3) experiments.

66 (CAD) and infrared multiphoton dissociation (IRMPD) of Ag-adducted phospholipids were investigated as

67 Infrared multiphoton dissociation (IRMPD) of alkali metal-coordinated oligosaccharides was

68 Infrared multiphoton dissociation (IRMPD) of deprotonated and protonated oligonucleotides r

69 Infrared multiphoton dissociation (IRMPD) of N-terminal sulfonated peptides improves de nov

70 selective infrared multiphoton dissociation (IRMPD) of S-sulfonated peptides in the background of unm

71 selective infrared multiphoton dissociation (IRMPD) of the cross-linked peptides.

72 performed infrared multiphoton dissociation (IRMPD) on 39 O-linked mucin-type oligosaccharide alditol

73 ng either infrared multiphoton dissociation (IRMPD) or multiple frequency sustained off-resonance irr

74 mpared to infrared multiphoton dissociation (IRMPD) or SORI-CID alone.

75 trometry, infrared multiphoton dissociation (IRMPD) spectroscopy, and DFT calculations.

76 he use of infrared multiphoton dissociation (IRMPD) to obtain structural information for large N-link

77 mparison, infrared multiphoton dissociation (IRMPD) was also applied to all oligosaccharide species.

78 Infrared multiphoton dissociation (IRMPD) was implemented in a novel dual pressure linear i

79 his work, infrared multiphoton dissociation (IRMPD) was interfaced with a commercial hybrid Qh-FT-ICR

80 ative ion infrared multiphoton dissociation (IRMPD) were employed to investigate the fragmentation of

81 on (CID), infrared multiphoton dissociation (IRMPD), and electron capture dissociation (ECD).

82 erized by infrared multiphoton dissociation (IRMPD), and the resulting spectra are compared to conven

83 I ECD) or infrared multiphoton dissociation (IRMPD), for the analysis of ubiquitinated proteins.

84 (ECD) and infrared multiphoton dissociation (IRMPD), in a 7-T Fourier transform ion cyclotron resonan

85 wn MS via infrared multiphoton dissociation (IRMPD), results in good sequence coverage enabling unamb

86 (CAD) or infrared multiphoton dissociation (IRMPD).

87 o ECD and infrared multiphoton dissociation (IRMPD).

88 mented by infrared multiphoton dissociation (IRMPD).

89 (CID) and infrared multiphoton dissociation (IRMPD).

90 , the infrared multiple photon dissociation (IRMPD) spectra of multiple peptide analytes are recorded

91 Infrared multiple photon dissociation (IRMPD) spectroscopy allows for the derivation of the vib

92 using infrared multiple photon dissociation (IRMPD) spectroscopy and theory.

93 using infrared multiple photon dissociation (IRMPD) spectroscopy between 800 and 3700 cm(-1), collisi

94 with infrared multiple photon dissociation (IRMPD) spectroscopy between 900 and 1850 cm(-1) and theo

95 Infrared multiple photon dissociation (IRMPD) spectroscopy combined with theoretical vibrationa

96 using infrared multiple photon dissociation (IRMPD) spectroscopy in conjunction with quantum chemical

97 Infrared multiple photon dissociation (IRMPD) spectroscopy of cis-[Pt(NH(3))(2)(G)Cl](+) and ci

98 ed by infrared multiple photon dissociation (IRMPD) spectroscopy using the free electron laser FELIX.

99 used infrared multiple photon dissociation (IRMPD) spectroscopy with mass spectrometry (MS-IR) to di

100 Infrared multiple photon dissociation (IRMPD) was used to generate vibrational spectra of ions

101 onant infrared multiple photon dissociation (IRMPD), has been applied for the identification of novel

102 d the infrared multiple photon dissociation (IRMPD), in order to build up cross-linked databases.

103 using infrared multiple photon dissociation (IRMPD).

104 ctive infrared multiple-photon dissociation (IRMPD).

105 Because of secondary dissociation, IRMPD yielded product ions in significantly lower charge

106 Not only does IRMPD promote highly efficient dissociation of the N-ter

107 n was partially overcome with a combined ECD/IRMPD approach (activated ion ECD).

108 Efficient IRMPD of both a 12-mer oligonucleotide and the protein m

109 were fragmented simultaneously using either IRMPD or SORI-CID techniques.

110 s present in crRNA and ATP molecules enhance IRMPD, an increase in the IR cross-section with the size

111 noncovalent adduct can substantially enhance IRMPD for nonphosphopeptides and that this strategy can

112 ss of the technique is demonstrated with ESI IRMPD FTICR mass spectrometry of a 20-mer phosphorothioa

113 The experimental IRMPD spectrum is reproduced with an appropriately weigh

114 Here, we explore IRMPD and EID of phosphate-containing metabolites and co

115 A comparison of the external IRMPD scheme with nozzle-skimmer dissociation and conven

116 reduction in dissociation energy facilitates IRMPD in a quadrupole ion trap.

117 q-value, irradiation time, and photon flux), IRMPD subtly, but significantly, outperforms resonant-ex

118 5 amino acid pairs, vs 66 for CAD and 50 for IRMPD in the FTMS cell.

119 ion of high power density to be employed for IRMPD.

120 The low pressure required for IRMPD (< or = 10(-5) Torr) is not that required for opti

121 the rich spectral information obtained from IRMPD and EID 2DMS contour plots can accurately identify

122 at 298 K, in agreement with the results from IRMPD spectroscopy.

123 In general, IRMPD and collisionally activated dissociation (CAD) pro

124 iable CAD experiments indicate that the high IRMPD efficiencies stem from the very large IR absorptiv

125 ) phosphate-containing metabolites; however, IRMPD generated more extensive fragmentation for larger

126 nucleobase ions can be observed directly in IRMPD experiments because the low-mass cutoff can be set

127 y contrast, glycosidic cleavages dominate in IRMPD although cross-ring fragmentation was also observe

128 iated with conventional CAD plays no role in IRMPD, resulting in richer MS/MS information in the low

129 are generally only low-intensity species in IRMPD spectra because nonresonant activation causes thes

130 positive ion IRMPD, AI-EDD and negative ion IRMPD provide complementary protein sequence information

131 Compared to AI-ECD and positive ion IRMPD, AI-EDD and negative ion IRMPD provide complementa

132 Visual comparison of experimental mid-IR IRMPD spectra and theoretical spectra could not establis

133 However, theoretical calculations, near-ir IRMPD spectra, and frequency-to-frequency and statistica

134 infrared-tunable free electron laser and its IRMPD spectrum recorded.

135 ng the 10.6 mum wavelength of a CO(2) laser, IRMPD suffers from the relative low absorption cross-sec

136 LC-IRMPD-MS proved to be an effective method to distinguish

137 ifications were identified using IRCX and LC-IRMPD-MS.

138 This LC-IRMPD-MS strategy is demonstrated for a mock mixture of

139 ermediates do not contribute to the measured IRMPD spectra.

140 We demonstrate this new IRMPD approach for the structural characterization of fl

141 The observed IRMPD spectrum of vapor-phase protonated parent matches

142 The application of IRMPD to the structural characterization of biochemical

143 s shown that the fragmentation efficiency of IRMPD increases with the increasing size of oligosacchar

144 erall, our work showcases the versatility of IRMPD in the top-down analysis of peptides, phosphopepti

145 is capillary heating has no effect on CAD or IRMPD of these ions collected in the FTMS cell.

146 fragments was greater than those from CID or IRMPD, and many ECD fragments contained the site(s) of n

147 nstrate the utility of FT-ICR with AI-ECD or IRMPD mass spectrometry in detecting SUMOylation, and si

148 alytical utility of performing either ECD or IRMPD on a given precursor ion population is demonstrate

149 Assignments were confirmed by AI ECD or IRMPD.

150 This scheme is unique from other IRMPD schemes as dissociation occurs in a spatially dist

151 For N-glycosylated tryptic peptides, IRMPD causes extensive cleavage of the glycosidic bonds,

152 veral posttranslationally modified peptides: IRMPD of phosphorylated peptides results in few backbone

153 opy, multiphoton infrared photodissociation (IRMPD) action spectroscopy, and density functional theor

154 Infrared multiphoton photodissociation (IRMPD) is combined with stored wave form inverse Fourier

155 For this reason IRMPD can sometimes facilitate analysis of sequences con

156 trap (dual-cell QLT) and perform large-scale IRMPD analyses of complex peptide mixtures.

157 sociation two-dimensional mass spectrometry (IRMPD 2DMS) is shown to be particularly effective.

158 rared multiphoton dissociation spectroscopy (IRMPD) to intermediates directly sampled from reaction m

159 increase MS/MS sensitivity, and a two-stage IRMPD/IRMPD method is demonstrated as a means to give sp

160 In this study, IRMPD of N-linked glycopeptides has been investigated wi

161 TA-IRMPD is performed with the bath gas at an elevated temp

162 ectively causes dissociation of all ions, TA-IRMPD can be made selective by using axial expansion to

163 d infrared multiphoton photodissociation (TA-IRMPD) provides an effective means to dissociate ions in

164 ontrast to previously reported accounts that IRMPD results only in glycosidic bond cleavage, the frag

165 We thus conclude that IRMPD performed in a dual-cell ion trap is an effective

166 We further demonstrate that IRMPD is compatible with the analysis of isobaric-tagged

167 able sequencing information, indicating that IRMPD is a viable alternative to CAD for oligonucleotide

168 ra of oligosaccharide alditols revealed that IRMPD could be used as a complementary method to obtain

169 We show that IRMPD activation parameters can be tuned to allow for ef

170 The IRMPD and CID behavior of oligosaccharides were compared

171 The IRMPD spectra clearly indicate that GlyArg x M(+), M = L

172 The IRMPD spectra clearly indicate that, for bases with GB v

173 The IRMPD spectra clearly indicate that, when Gly, Val, Pro,

174 The IRMPD spectra for these ions exhibit bands assigned to c

175 The IRMPD spectra of arginine complexed with divalent stront

176 The IRMPD spectra of cis-[Pt(NH(3))(2)(A)Cl](+) are consiste

177 The IRMPD spectrum of protonated PhePhe is reproduced with g

178 calculated for low-energy structures and the IRMPD spectra of analogous ions containing monovalent al

179 an branch sites could be determined from the IRMPD fragments.

180 r than 90% of the product ion current in the IRMPD mass spectra of doubly charged peptide ions was co

181 There are only subtle differences in the IRMPD spectra for dipeptides containing Gly, Val, Pro, a

182 We then evaluate the impact of size on the IRMPD of proteins and their complexes.

183 secondary product ions, thus simplifying the IRMPD product ion mass spectra.

184 he helium pressure is not detrimental to the IRMPD experiment when nominal pressures lower than 2 x 1

185 nment that is confirmed by comparison to the IRMPD spectrum of (HisArg x H(2))(2+).

186 rmation was obtained with ECD as compared to IRMPD.

187 corresponding to the loss of phosphate under IRMPD fragmentation allows the selective identification

188 date the site of covalent drug bonding using IRMPD for a mixture of epidermal growth factor receptor

189 ence coverage of peptides was obtained using IRMPD over CID.

190 r ions, but necessitates the use of variable IRMPD irradiation times, dependent upon precursor mass t

191 e source of information for fixed wavelength IRMPD exploited in dissociation protocols of peptides an

192 When IRMPD was performed in the high pressure cell, most pept

193 nstrated on an ESI-FTICR instrument in which IRMPD is performed in the external ion reservoir and on

194 pletely sequence the oligosaccharides, while IRMPD of the same compounds yielded the fragment ions co

195 y N-terminal sulfonation in combination with IRMPD provided significant improvements in sequence iden

196 ated peptide ion, Ac-VQIVYK(H(+))-NHMe, with IRMPD spectroscopy in the fingerprint and amide I/II ban