메뉴 건너뛰기




Volumn 23, Issue 10, 2012, Pages 1707-1715

Systematic comparison of ultraviolet photodissociation and electron transfer dissociation for peptide anion characterization

Author keywords

Negative electron transfer dissociation; Protein identification; Tandem mass spectrometry; Ultraviolet photodissociation

Indexed keywords

CHARGE STATE; CHARGED SPECIES; CLEAVAGE PREFERENCE; COVERAGE PERCENTAGE; DATABASE SEARCHING; DIAGNOSTIC INFORMATION; ELECTRON TRANSFER DISSOCIATION; HETEROGENEOUS ARRAY; HIGH PH; ION SIGNALS; MOBILE PHASIS; PEPTIDE ANIONS; PEPTIDE BACKBONES; PEPTIDE IDENTIFICATION; POSITIVE MODE; PROTEIN DIGESTS; PROTEIN IDENTIFICATION; PROTEOMES; RAPID ACTIVATION; TANDEM MASS SPECTROMETRY; ULTRAVIOLET PHOTODISSOCIATION;

EID: 84868235717     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-012-0424-9     Document Type: Article
Times cited : (28)

References (50)
  • 1
    • 0019618203 scopus 로고
    • Sequence analysis of polypeptides by collision activated dissociation on a triple quadrupole mass spectrometer
    • Hunt, D.F., Buko, A.M., Ballard, J.M., Shabanowitz, J., Giordani, A.B.: Sequence analysis of polypeptides by collision activated dissociation on a triple quadrupole mass spectrometer. Biol. Mass Spectrom. 8, 397-408 (1981)
    • (1981) Biol. Mass Spectrom. , vol.8 , pp. 397-408
    • Hunt, D.F.1    Buko, A.M.2    Ballard, J.M.3    Shabanowitz, J.4    Giordani, A.B.5
  • 2
    • 0005387475 scopus 로고
    • Principles of collisional activation in analytical mass spectrometry
    • McLuckey, S.: Principles of collisional activation in analytical mass spectrometry. J. Am. Soc. Mass Spectrom. 3, 599-614 (1992)
    • (1992) J. Am. Soc. Mass Spectrom. , vol.3 , pp. 599-614
    • McLuckey, S.1
  • 3
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J.K., McCormack, A.L., Yates III, J.R.: An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989 (1994)
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 4
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D.N., Pappin, D.J.C., Creasy, D.M., Cottrell, J.S.: Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (1999)
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 6
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • Zubarev, R.A., Kelleher, N.L., McLafferty, F.W.: Electron capture dissociation of multiply charged protein cations. A nonergodic process. J. Am. Chem. Soc. 120, 3265-3266 (1998)
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 7
    • 0033214591 scopus 로고    scopus 로고
    • Localization of labile post-translational modifications by electron capture dissociation: The case of γ-carboxyglutamic acid
    • Kelleher, N.L., Zubarev, R.A., Bush, K., Furie, B., Furie, B.C., McLafferty, F.W., Walsh, C.T.: Localization of labile post-translational modifications by electron capture dissociation: the case of γ- carboxyglutamic acid. Anal. Chem. 71, 4250-4253 (1999)
    • (1999) Anal. Chem. , vol.71 , pp. 4250-4253
    • Kelleher, N.L.1    Zubarev, R.A.2    Bush, K.3    Furie, B.4    Furie, B.C.5    McLafferty, F.W.6    Walsh, C.T.7
  • 9
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J.E.P., Coon, J.J., Schroeder, M.J., Shabanowitz, J., Hunt, D.F.: Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. PNAS 101, 9528-9533 (2004)
    • (2004) PNAS , vol.101 , pp. 9528-9533
    • Syka, J.E.P.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 10
    • 4344683981 scopus 로고    scopus 로고
    • Anion dependence in the partitioning between proton and electron transfer in ion/ion reactions
    • Coon, J.J., Syka, J.E.P., Schwartz, J.C., Shabanowitz, J., Hunt, D.F.: Anion dependence in the partitioning between proton and electron transfer in ion/ion reactions. Int. J. Mass Spectrom. 236, 33-42 (2004)
    • (2004) Int. J. Mass Spectrom. , vol.236 , pp. 33-42
    • Coon, J.J.1    Syka, J.E.P.2    Schwartz, J.C.3    Shabanowitz, J.4    Hunt, D.F.5
  • 11
    • 36749068401 scopus 로고    scopus 로고
    • Performance characteristics of electron transfer dissociation mass spectrometry
    • Good, D.M., Wirtala, M., McAlister, G.C., Coon, J.J.: Performance characteristics of electron transfer dissociation mass spectrometry. Mol. Cell. Proteom. 6, 1942-1951 (2007)
    • (2007) Mol. Cell. Proteom. , vol.6 , pp. 1942-1951
    • Good, D.M.1    Wirtala, M.2    McAlister, G.C.3    Coon, J.J.4
  • 12
    • 0000948847 scopus 로고
    • Fragmentation of oligopeptide ions using ultraviolet laser radiation and fourier transform mass spectrometry
    • Bowers, W.D., Delbert, S.S., Hunter, R.L., McIver, R.T.: Fragmentation of oligopeptide ions using ultraviolet laser radiation and Fourier transform mass spectrometry. J. Am. Chem. Soc. 106, 7288-7289 (1984)
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 7288-7289
    • Bowers, W.D.1    Delbert, S.S.2    Hunter, R.L.3    McIver, R.T.4
  • 13
    • 0027997748 scopus 로고
    • Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing
    • Little, D.P., Speir, J.P., Senko, M.W., O'Connor, P.B., McLafferty, F.W.: Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing. Anal. Chem. 66, 2809-2815 (1994)
    • (1994) Anal. Chem. , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    O'Connor, P.B.4    McLafferty, F.W.5
  • 14
    • 0033152778 scopus 로고    scopus 로고
    • Infrared multiphoton dissociation in an external ion reservoir
    • Hofstadler, S.A., Sannes-Lowery, K.A., Griffey, R.H.: Infrared multiphoton dissociation in an external ion reservoir. Anal. Chem. 71, 2067-2070 (1999)
    • (1999) Anal. Chem. , vol.71 , pp. 2067-2070
    • Hofstadler, S.A.1    Sannes-Lowery, K.A.2    Griffey, R.H.3
  • 15
    • 33749476335 scopus 로고    scopus 로고
    • Infrared multiphoton dissociation for enhanced de novo sequence interpretation of N-terminal sulfonated peptides in a quadrupole ion trap
    • Wilson, J.J., Brodbelt, J.S.: Infrared multiphoton dissociation for enhanced de novo sequence interpretation of N-terminal sulfonated peptides in a quadrupole ion trap. Anal. Chem. 78, 6855-6862 (2006)
    • (2006) Anal. Chem. , vol.78 , pp. 6855-6862
    • Wilson, J.J.1    Brodbelt, J.S.2
  • 17
    • 20644461905 scopus 로고    scopus 로고
    • Peptide photodissociation at 157 nm in a linear ion trap mass spectrometer
    • Kim, T.-Y., Thompson, M.S., Reilly, J.P.: Peptide photodissociation at 157 nm in a linear ion trap mass spectrometer. Rapid Commun. Mass Spectrom. 19, 1657-1665 (2005)
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 1657-1665
    • Kim, T.-Y.1    Thompson, M.S.2    Reilly, J.P.3
  • 18
    • 70349917570 scopus 로고    scopus 로고
    • Ultraviolet photodissociation: Developments towards applications for mass-spectrometry-based proteomics
    • Ly, T., Julian, R.R.: Ultraviolet photodissociation: developments towards applications for mass-spectrometry-based proteomics. Angew. Chem. Int. Ed. 48, 7130-7137 (2009)
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 7130-7137
    • Ly, T.1    Julian, R.R.2
  • 19
    • 66149151341 scopus 로고    scopus 로고
    • Ultraviolet photofragmentation of biomolecular ions
    • Reilly, J.P.: Ultraviolet photofragmentation of biomolecular ions. Mass Spectrom. Rev. 28, 425-447 (2009)
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 425-447
    • Reilly, J.P.1
  • 20
    • 38349064873 scopus 로고    scopus 로고
    • Residue-specific radical-directed dissociation of whole proteins in the gas phase
    • Ly, T., Julian, R.R.: Residue-specific radical-directed dissociation of whole proteins in the gas phase. J. Am. Chem. Soc. 130, 351-358 (2008)
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 351-358
    • Ly, T.1    Julian, R.R.2
  • 21
    • 33646112403 scopus 로고    scopus 로고
    • Comparative studies of 193-nm photodissociation and TOF-TOFMS analysis of bradykinin analogues: The effects of charge site(s) and fragmentation timescales
    • Morgan, J.W., Russell, D.H.: Comparative studies of 193-nm photodissociation and TOF-TOFMS analysis of bradykinin analogues: the effects of charge site(s) and fragmentation timescales. J. Am. Soc. Mass Spectrom. 17, 721-729 (2006)
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 721-729
    • Morgan, J.W.1    Russell, D.H.2
  • 22
    • 34447636243 scopus 로고    scopus 로고
    • Factors that impact the vacuum ultraviolet photofragmentation of peptide ions
    • Thompson, M.S., Cui, W., Reilly, J.P.: Factors that impact the vacuum ultraviolet photofragmentation of peptide ions. J. Am. Soc. Mass Spectrom. 18, 1439-1452 (2007)
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1439-1452
    • Thompson, M.S.1    Cui, W.2    Reilly, J.P.3
  • 23
    • 70449486708 scopus 로고    scopus 로고
    • Time-resolved observation of product ions generated by 157 nm photodissociation of singly protonated phosphopeptides
    • Kim, T.-Y., Reilly, J.P.: Time-resolved observation of product ions generated by 157 nm photodissociation of singly protonated phosphopeptides. J. Am. Soc. Mass Spectrom. 20, 2334-2341 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 2334-2341
    • Kim, T.-Y.1    Reilly, J.P.2
  • 24
    • 77955435456 scopus 로고    scopus 로고
    • Ultrafast ultraviolet photodissociation at 193 nm and its applicability to proteomic workflows
    • Madsen, J.A., Boutz, D.R., Brodbelt, J.S.: Ultrafast ultraviolet photodissociation at 193 nm and its applicability to proteomic workflows. J. Proteome Res. 9, 4205-4214 (2010)
    • (2010) J. Proteome Res. , vol.9 , pp. 4205-4214
    • Madsen, J.A.1    Boutz, D.R.2    Brodbelt, J.S.3
  • 25
    • 73449138220 scopus 로고    scopus 로고
    • Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides
    • Shin, Y.S., Moon, J.H., Kim, M.S.: Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides. J. Am. Soc. Mass Spectrom. 21, 53-59 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 53-59
    • Shin, Y.S.1    Moon, J.H.2    Kim, M.S.3
  • 26
    • 79952522401 scopus 로고    scopus 로고
    • Shedding light on the frontier of photodissociation
    • Brodbelt, J.S.: Shedding light on the frontier of photodissociation. J. Am. Soc. Mass Spectrom. 22, 197-206 (2001)
    • (2001) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 197-206
    • Brodbelt, J.S.1
  • 27
    • 42749090263 scopus 로고    scopus 로고
    • Time-resolved photodissociation of singly protonated peptides with an arginine at the N-terminus: A statistical interpretation
    • Time-resolved photodissociation of singly protonated peptides with an arginine at the N-terminus: a statistical interpretation. J. Am. Soc. Mass Spectrom. 19, 645-655 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 645-655
  • 28
    • 0034845380 scopus 로고    scopus 로고
    • Phosphopeptide analysis by positive and negative ion matrix-assisted laser desorption/ionization mass spectrometry
    • Janek, K., Wenschuh, H., Bienert, M., Krause, E.: Phosphopeptide analysis by positive and negative ion matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 15, 1593-1599 (2001)
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1593-1599
    • Janek, K.1    Wenschuh, H.2    Bienert, M.3    Krause, E.4
  • 29
    • 33744901953 scopus 로고    scopus 로고
    • Phosphopeptide anion characterization via sequential charge inversion and electron-transfer dissociation
    • Gunawardena, H.P., Emory, J.F., McLuckey, S.A.: Phosphopeptide anion characterization via sequential charge inversion and electron-transfer dissociation. Anal. Chem. 78, 3788-3793 (2006)
    • (2006) Anal. Chem. , vol.78 , pp. 3788-3793
    • Gunawardena, H.P.1    Emory, J.F.2    McLuckey, S.A.3
  • 30
    • 0035566890 scopus 로고    scopus 로고
    • Dissociation of multiply charged negative ions for hirudin (54-65), fibrinopeptide B, and insulin A (oxidized)
    • Ewing, N., Cassady, C.: Dissociation of multiply charged negative ions for hirudin (54-65), fibrinopeptide B, and insulin A (oxidized). J. Am. Soc. Mass Spectrom. 12, 105-116 (2001)
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 105-116
    • Ewing, N.1    Cassady, C.2
  • 31
    • 0036489424 scopus 로고    scopus 로고
    • - parent anions of underivatized peptides: An aid to structure determination and some unusual negative ion cleavages
    • - parent anions of underivatized peptides: An aid to structure determination and some unusual negative ion cleavages. Mass Spectrom. Rev. 21, 87-107 (2002)
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 87-107
    • Bowie, J.H.1    Brinkworth, C.S.2    Dua, S.3
  • 32
    • 0030978273 scopus 로고    scopus 로고
    • - ions derived from caeridin and dynastin peptides. Internal backbone cleavages directed through asp and asn residues
    • - ions derived from caeridin and dynastin peptides. Internal backbone cleavages directed through Asp and Asn residues. Rapid Commun. Mass Spectrom. 11, 253-258 (1997)
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 253-258
    • Steinborner, S.T.1    Bowie, J.H.2
  • 33
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • Jensen, O.N.: Interpreting the protein language using proteomics. Nat. Rev. Mol. Cell. Biol. 7, 391-403 (2006)
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 391-403
    • Jensen, O.N.1
  • 34
    • 0034744173 scopus 로고    scopus 로고
    • Whole proteome pI values correlate with subcellular localizations of proteins for organisms within the three domains of life
    • Schwartz, R., Ting, C.S., King, J.: Whole proteome pI values correlate with subcellular localizations of proteins for organisms within the three domains of life. Genome Res. 11, 703-709 (2001)
    • (2001) Genome Res. , vol.11 , pp. 703-709
    • Schwartz, R.1    Ting, C.S.2    King, J.3
  • 35
    • 2942567744 scopus 로고    scopus 로고
    • Global analysis of predicted proteomes: Functional adaptation of physical properties
    • Knight, C.G., Kassen, R., Hebestreit, H., Rainey, P.B.: Global analysis of predicted proteomes: functional adaptation of physical properties. Proc. Nat. Acad. Sci. U.S.A. 101, 8390-8395 (2004)
    • (2004) Proc. Nat. Acad. Sci. USA , vol.101 , pp. 8390-8395
    • Knight, C.G.1    Kassen, R.2    Hebestreit, H.3    Rainey, P.B.4
  • 36
    • 1842476119 scopus 로고    scopus 로고
    • The modal distribution of protein isoelectric points reflects amino acid properties rather than sequence evolution
    • Weiller, G.F., Caraux, G., Sylvester, N.: The modal distribution of protein isoelectric points reflects amino acid properties rather than sequence evolution. Proteomics 4, 943-949 (2004)
    • (2004) Proteomics , vol.4 , pp. 943-949
    • Weiller, G.F.1    Caraux, G.2    Sylvester, N.3
  • 38
    • 15044352515 scopus 로고    scopus 로고
    • Cα-C backbone fragmentation dominates in electron detachment dissociation of gas-phase polypeptide polyanions
    • Kjeldsen, F., Silivra, O.A., Ivonin, I.A., Haselmann, K.F., Gorshkov, M., Zubarev, R.A.: Cα-C Backbone Fragmentation Dominates in Electron Detachment Dissociation of Gas-Phase Polypeptide Polyanions. Chem. Eur. J. 11, 1803-1812 (2005)
    • (2005) Chem. Eur. J. , vol.11 , pp. 1803-1812
    • Kjeldsen, F.1    Silivra, O.A.2    Ivonin, I.A.3    Haselmann, K.F.4    Gorshkov, M.5    Zubarev, R.A.6
  • 39
    • 48349085761 scopus 로고    scopus 로고
    • Towards liquid chromatography time-scale peptide sequencing and characterization of post-translational modifications in the negativeion mode using electron detachment dissociation tandem mass spectrometry
    • Kjeldsen, F., Horning, O.B., Jensen, S.S., Giessing, A.M.B., Jensen, O.N.: Towards liquid chromatography time-scale peptide sequencing and characterization of post-translational modifications in the negativeion mode using electron detachment dissociation tandem mass spectrometry. J. Am. Soc. Mass Spectrom. 19, 1156-1162 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1156-1162
    • Kjeldsen, F.1    Horning, O.B.2    Jensen, S.S.3    Giessing, A.M.B.4    Jensen, O.N.5
  • 41
    • 79955823384 scopus 로고    scopus 로고
    • Metastable atom-activated dissociation mass spectrometry of phosphorylated and sulfonated peptides in negative ion mode
    • Cook, S., Jackson, G.: Metastable atom-activated dissociation mass spectrometry of phosphorylated and sulfonated peptides in negative ion mode. J. Am. Soc. Mass Spectrom. 22, 1088-1099 (2011)
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1088-1099
    • Cook, S.1    Jackson, G.2
  • 42
    • 77950372664 scopus 로고    scopus 로고
    • Negative electron transfer dissociation of deprotonated phosphopeptide anions: Choice of radical cation reagent and competition between electron and proton transfer
    • Huzarska, M., Ugalde, I., Kaplan, D.A., Hartmer, R., Easterling, M.L., Polfer, N.C.: Negative electron transfer dissociation of deprotonated phosphopeptide anions: choice of radical cation reagent and competition between electron and proton transfer. Anal. Chem. 82, 2873-2878 (2010)
    • (2010) Anal. Chem. , vol.82 , pp. 2873-2878
    • Huzarska, M.1    Ugalde, I.2    Kaplan, D.A.3    Hartmer, R.4    Easterling, M.L.5    Polfer, N.C.6
  • 44
    • 79953035693 scopus 로고    scopus 로고
    • 193-nm photodissociation of singly and multiply charged peptide anions for acidic proteome characterization
    • Madsen, J.A., Kaoud, T.S., Dalby, K.N., Brodbelt, J.S.: 193-nm photodissociation of singly and multiply charged peptide anions for acidic proteome characterization. Proteomics 11, 1329-1334 (2011)
    • (2011) Proteomics , vol.11 , pp. 1329-1334
    • Madsen, J.A.1    Kaoud, T.S.2    Dalby, K.N.3    Brodbelt, J.S.4
  • 45
    • 33846188053 scopus 로고    scopus 로고
    • Photo-induced formation of radical anion peptides. Electron photodetachment dissociation experiments
    • Antoine, R., Joly, L., Tabarin, T., Broyer, M., Dugourd, P., Lemoine, J.: Photo-induced formation of radical anion peptides. Electron photodetachment dissociation experiments. Rapid Commun. Mass Spectrom 21, 265-268 (2007)
    • (2007) Rapid Commun. Mass Spectrom , vol.21 , pp. 265-268
    • Antoine, R.1    Joly, L.2    Tabarin, T.3    Broyer, M.4    Dugourd, P.5    Lemoine, J.6
  • 48
    • 34249094851 scopus 로고    scopus 로고
    • A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data
    • Xu, H., Freitas, M.: A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data. BMC Bioinformatics 8, 133 (2007)
    • (2007) BMC Bioinformatics , vol.8 , pp. 133
    • Xu, H.1    Freitas, M.2
  • 49
    • 38649131282 scopus 로고    scopus 로고
    • Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine
    • Xu, H., Zhang, L., Freitas, M.A.: Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine. J. Proteome Res. 7, 138-144 (2008)
    • (2008) J. Proteome Res. , vol.7 , pp. 138-144
    • Xu, H.1    Zhang, L.2    Freitas, M.A.3
  • 50
    • 77954356041 scopus 로고    scopus 로고
    • Database search algorithm for identification of intact cross-links in proteins and peptides using tandem mass spectrometry
    • Xu, H., Hsu, P.-H., Zhang, L., Tsai, M.-D., Freitas, M.A.: Database search algorithm for identification of intact cross-links in proteins and peptides using tandem mass spectrometry. J. Proteome Res. 9, 3384-3393 (2010)
    • (2010) J. Proteome Res. , vol.9 , pp. 3384-3393
    • Xu, H.1    Hsu, P.-H.2    Zhang, L.3    Tsai, M.-D.4    Freitas, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.