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 yielded comparable information to previously repor

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

11 ations in resonant frequencies do not affect IRMPD.

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

13 Also, IRMPD showed an increased selectivity toward backbone cl

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

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

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

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

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

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

20 CID and IRMPD spectra of several oligosaccharides were also comp

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

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

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

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

25 n fully characterized by CID experiments and IRMPD spectroscopy.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

47 10.6-mum infrared multiphoton dissociation (IRMPD) for the characterization of lipid A structures wa

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

75 o ECD and infrared multiphoton dissociation (IRMPD).

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

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

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

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

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

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

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

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

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

85 ctive infrared multiple-photon dissociation (IRMPD).

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

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

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

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

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

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

92 The experimental IRMPD spectrum is reproduced with an appropriately weigh

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

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

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

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

97 5 amino acid pairs, vs 66 for CAD and 50 for IRMPD in the FTMS cell.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

116 ermediates do not contribute to the measured IRMPD spectra.

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

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

119 The application of IRMPD to the structural characterization of biochemical

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

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

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

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

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

125 Assignments were confirmed by AI ECD or IRMPD.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

145 The IRMPD and CID behavior of oligosaccharides were compared

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

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

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

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

150 The IRMPD spectra of arginine complexed with divalent stront

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

152 The IRMPD spectrum of protonated PhePhe is reproduced with g

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

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

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

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

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

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

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

160 rmation was obtained with ECD as compared to IRMPD.

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

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

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

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

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

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

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

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