메뉴 건너뛰기




Volumn 10, Issue 5, 2011, Pages 2318-2329

Using ion mobility data to improve peptide identification: Intrinsic amino acid size parameters

Author keywords

ion mobility spectrometry; mass spectrometry; peptide identification

Indexed keywords

AMINO ACID; PEPTIDE DERIVATIVE;

EID: 79955870883     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr1011312     Document Type: Article
Times cited : (53)

References (72)
  • 1
    • 0023655503 scopus 로고
    • Peptide sequencing by magnetic deflection tandem mass spectrometry
    • Scoble, H. A.; Martin, S. A.; Biemann, K. Peptide sequencing by magnetic deflection tandem mass spectrometry Biochem. J. 1987, 245, 621-622
    • (1987) Biochem. J. , vol.245 , pp. 621-622
    • Scoble, H.A.1    Martin, S.A.2    Biemann, K.3
  • 2
    • 0002794845 scopus 로고    scopus 로고
    • Collision induced fragmentation of (M+H)+ ions of peptides. Side chain specific sequence
    • Johnson, R. S; Martin, S. A.; Biemann, K. Collision induced fragmentation of (M+H)+ ions of peptides. Side chain specific sequence Int. J. Mass Spectrom. Ion Processes 1998, 86, 137-154
    • (1998) Int. J. Mass Spectrom. Ion Processes , vol.86 , pp. 137-154
    • Johnson, R.S.1    Martin, S.A.2    Biemann, K.3
  • 4
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • DOI 10.1021/ac010617e
    • Wolters, D. A.; Washburn, M. P.; Yates, J. R. An Automated Multidimensional Protein Identification Technology for Shotgun Proteomics Anal. Chem. 2001, 73, 5683-5690 (Pubitemid 33126725)
    • (2001) Analytical Chemistry , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 5
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn, M. P.; Wolters, D.; Yates, J. R. Large-Scale Analysis of the Yeast Proteome by Multidimensional Protein Identification Technology Nat. Biotechnol. 2001, 19, 242-247 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 6
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • DOI 10.1021/pr025556v
    • Peng, J.; Elias, J. E.; Thoreen, C. C.; Licklider, L. J.; Gygi, S. P. Evaluation of Multidimensional Chromatography Coupled with Tandem Mass Spectrometry (LC/LC-MS/MS) for Large-Scale Protein Analysis: The Yeast Proteome J. Proteome Res. 2003, 2, 43-50 (Pubitemid 36207189)
    • (2003) Journal of Proteome Research , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 8
    • 0041733300 scopus 로고    scopus 로고
    • Evaluation of shotgun sequencing for proteomic analysis of human plasma using HPLC coupled with either ion trap or Fourier transform mass spectrometry
    • DOI 10.1021/pr034015i
    • Wu, S. L.; Choudhary, G.; Ramstrom, M.; Bergquist, J.; Hancock, W. S. Evaluation of Shotgun Sequencing for Proteomic Analysis of Human Plasma Using HPLC Coupled with either Ion Trap or Fourier Transform Mass Spectrometry J. Proteome Res. 2003, 2, 383-393 (Pubitemid 36988417)
    • (2003) Journal of Proteome Research , vol.2 , Issue.4 , pp. 383-393
    • Wu, S.-L.1    Choudhary, G.2    Ramstrom, M.3    Bergquist, J.4    Hancock, W.S.5
  • 10
    • 1242316198 scopus 로고    scopus 로고
    • Ultra-High-Efficiency Strong Cation Exchange LC/RPLC/MS/MS for High Dynamic Range Characterization of the Human Plasma Proteome
    • DOI 10.1021/ac034869m
    • Shen, Y.; Jacobs, J. M.; Camp, D. G., II; Fang, R.; Moore, R. J.; Smith, R. D.; Xiao, W.; Davis, R. W.; Tompkins, R. G. Ultra-High-Efficiency Strong Cation Exchange LC/RPLC/MS/MS for High Dynamic Range Characterization of the Human Plasma Proteome Anal. Chem. 2004, 76, 1134-1144 (Pubitemid 38235564)
    • (2004) Analytical Chemistry , vol.76 , Issue.4 , pp. 1134-1144
    • Shen, Y.1    Jacobs, J.M.2    Camp II, D.G.3    Fang, R.4    Moore, R.J.5    Smith, R.D.6    Xiao, W.7    Davis, R.W.8    Tompkins, R.G.9
  • 13
    • 38649126540 scopus 로고    scopus 로고
    • What's driving false discovery rates?
    • DOI 10.1021/pr700728t
    • Tabb, D. L. What's driving the false discovery rate? J. Proteome Res. 2008, 7, 45-46 (Pubitemid 351171113)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 45-46
    • Tabb, D.L.1
  • 14
    • 34547732831 scopus 로고    scopus 로고
    • Using statistical models to identify factors that have a role in defining the abundance of ions produced by tandem MS
    • DOI 10.1021/ac0700272
    • Barton, S.; Richardson, S.; Perkins, D.; Bellahn, I.; Bryant, T.; Whittaker, J. Using Statistical Models To Identify Factors That Have a Role in Defining the Abundance of Ions Produced by Tandem MS Anal. Chem. 2007, 79, 5601-5607 (Pubitemid 47229805)
    • (2007) Analytical Chemistry , vol.79 , Issue.15 , pp. 5601-5607
    • Barton, S.J.1    Richardson, S.2    Perkins, D.N.3    Bellahn, I.4    Bryant, T.N.5    Whittaker, J.C.6
  • 15
    • 0346158344 scopus 로고    scopus 로고
    • Deriving statistical models for predicting peptide tandem MS product ion intensities
    • Schutz, F.; Kapp, E.; Simpson, R.; Speed, T. Deriving statistical models for predicting peptide tandem MS product ion intensities Biochem. Soc. Trans. 2003, 31, 1479-1483 (Pubitemid 38031006)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1479-1483
    • Schutz, F.1    Kapp, E.A.2    Simpson, R.J.3    Speed, T.P.4
  • 16
    • 0742305695 scopus 로고    scopus 로고
    • Intensity-based protein identification by machine learning from a library of tandem mass spectra
    • DOI 10.1038/nbt930
    • Elias, J.; Gibbons, F.; King, O.; Roth, F.; Gygi, S. Intensity-based protein identification by machine learning from a library of tandem mass spectra Nat. Biotechnol. 2004, 22, 214-219 (Pubitemid 38160538)
    • (2004) Nature Biotechnology , vol.22 , Issue.2 , pp. 214-219
    • Elias, J.E.1    Gibbons, F.D.2    King, O.D.3    Roth, F.P.4    Gygi, S.P.5
  • 17
    • 13844319908 scopus 로고    scopus 로고
    • PepNovo: De novo peptide sequencing via probabilistic network modeling
    • DOI 10.1021/ac048788h
    • Frank, A.; Pevzner, P. PepNovo: De Novo Peptide Sequencing via Probabilistic Network Modeling Anal. Chem. 2005, 77, 964-973 (Pubitemid 40261761)
    • (2005) Analytical Chemistry , vol.77 , Issue.4 , pp. 964-973
    • Frank, A.1    Pevzner, P.2
  • 18
    • 27544511899 scopus 로고    scopus 로고
    • InsPecT: Identification of posttranslationally modified peptides from tandem mass spectra
    • DOI 10.1021/ac050102d
    • Tanner, S.; Shu, H.; Frank, A.; Mumby, M.; Pevzner, P.; Bafna, V. InsPecT: Fast and accurate identification of post-translationally modified peptides from tandem mass spectra Anal. Chem. 2005, 77, 4626-4639 (Pubitemid 41542287)
    • (2005) Analytical Chemistry , vol.77 , Issue.14 , pp. 4626-4639
    • Tanner, S.1    Shu, H.2    Frank, A.3    Wang, L.-C.4    Zandi, E.5    Mumby, M.6    Pevzner, P.A.7    Bafna, V.8
  • 19
    • 30744444934 scopus 로고    scopus 로고
    • PepHMM: A hidden Markov model based scoring function for mass spectrometry database search
    • DOI 10.1021/ac051319a
    • Wan, Y.; Chen, T. PepHMM: A hidden Markov model based scoring function for tandem mass spectrometry Anal. Chem. 2006, 78, 432-437 (Pubitemid 43100374)
    • (2006) Analytical Chemistry , vol.78 , Issue.2 , pp. 432-437
    • Wan, Y.1    Yang, A.2    Chen, T.3
  • 20
    • 33847234661 scopus 로고    scopus 로고
    • Lookup Peaks: A Hybrid of de Novo Sequencing and Database Search for Protein Identification by Tandem Mass Spectrometry
    • Bern, M.; Cai, Y.; Goldberg, D. Lookup Peaks: A Hybrid of de Novo Sequencing and Database Search for Protein Identification by Tandem Mass Spectrometry Anal. Chem. 2007, 79, 1393-1400
    • (2007) Anal. Chem. , vol.79 , pp. 1393-1400
    • Bern, M.1    Cai, Y.2    Goldberg, D.3
  • 21
    • 35349021975 scopus 로고    scopus 로고
    • Peptide fragment intensity statistical modeling
    • DOI 10.1021/ac070488n
    • Colinge, J. Peptide Fragment Intensity Statistical Modeling Anal. Chem. 2007, 79, 7286-7290 (Pubitemid 47606094)
    • (2007) Analytical Chemistry , vol.79 , Issue.19 , pp. 7286-7290
    • Colinge, J.1
  • 22
    • 46249088907 scopus 로고    scopus 로고
    • Modeling peptide fragmentation with dynamic Bayesian networks for peptide identification
    • Klammer, A.; Reynolds, S.; Bilmes, J.; MacCoss, M.; Noble, W. Modeling peptide fragmentation with dynamic Bayesian networks for peptide identification Bioinformatics 2008, 24, i348-356
    • (2008) Bioinformatics , vol.24 , pp. 348-356
    • Klammer, A.1    Reynolds, S.2    Bilmes, J.3    MacCoss, M.4    Noble, W.5
  • 23
    • 3242660851 scopus 로고    scopus 로고
    • Prediction of low-energy collision-induced dissociation spectra of peptides
    • DOI 10.1021/ac049951b
    • Zhang, Z. Prediction of Low-Energy Collision-Induced Dissociation Spectra of Peptides Anal. Chem. 2004, 76, 3908-3922 (Pubitemid 38943659)
    • (2004) Analytical Chemistry , vol.76 , Issue.14 , pp. 3908-3922
    • Zhang, Z.1
  • 24
    • 26444607864 scopus 로고    scopus 로고
    • Prediction of low-energy collision-induced dissociation spectra of peptides with three or more charges
    • DOI 10.1021/ac050857k
    • Zhang, Z. Prediction of Low-Energy Collision-Induced Dissociation Spectra of Peptides with Three or More Charges Anal. Chem. 2005, 77, 6364-6373 (Pubitemid 41436975)
    • (2005) Analytical Chemistry , vol.77 , Issue.19 , pp. 6364-6373
    • Zhang, Z.1
  • 25
    • 66749169317 scopus 로고    scopus 로고
    • Predicting Intensity Ranks of Peptide Fragment Ions
    • Frank, A. M. Predicting Intensity Ranks of Peptide Fragment Ions J. Proteome Res. 2009, 8, 2226-2240
    • (2009) J. Proteome Res. , vol.8 , pp. 2226-2240
    • Frank, A.M.1
  • 28
    • 5744223586 scopus 로고    scopus 로고
    • An improved model for prediction of retention times of tryptic peptides in ion pair reversed-phase HPLC: Its application to protein peptide mapping by off-line HPLC-MALDI MS
    • DOI 10.1074/mcp.M400031-MCP200
    • Krokhin, O. V.; Craig, R.; Spicer, V.; Ens, W.; Standing, K. G.; Beavis, R. C.; Wilkins, J. A. An Improved Model for Prediction of Retention Times of Tryptic Peptides in Ion Pair Reversed-phase HPLC Its Application to Protein Peptide Mapping by Off-Line HPLC-MALDI MS Mol. Cell. Proteomics 2004, 3.9, 908-919 (Pubitemid 39377699)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.9 , pp. 908-919
    • Krokhin, O.V.1    Craig, R.2    Spicer, V.3    Ens, W.4    Standing, K.G.5    Beavis, R.C.6    Wilkins, J.A.7
  • 30
    • 0037112383 scopus 로고    scopus 로고
    • Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry
    • DOI 10.1021/ac0256890
    • Palmblad, M.; Ramstrom, M.; Markides, K. E.; Hakansson, P.; Bergquist, J. Prediction of chromatographic retention and protein identification in liquid chromatography/mass spectrometry Anal. Chem. 2002, 74, 5826-5830 (Pubitemid 35364839)
    • (2002) Analytical Chemistry , vol.74 , Issue.22 , pp. 5826-5830
    • Palmblad, M.1    Ramstrom, M.2    Markides, K.E.3    Hakansson, P.4    Bergquist, J.5
  • 31
    • 33845889721 scopus 로고    scopus 로고
    • Neural network prediction of peptide separation in strong anion exchange chromatography
    • DOI 10.1093/bioinformatics/btl561
    • Oh, C.; Zak, S. H.; Mirzaei, H.; Buck, C.; Regnier, F. E.; Zhang, X. Neural network prediction of peptide separation in strong anion exchange chromatography Bioinformatics 2007, 23 (1) 114-118 (Pubitemid 46017863)
    • (2007) Bioinformatics , vol.23 , Issue.1 , pp. 114-118
    • Oh, C.1    Zak, S.H.2    Mirzaei, H.3    Buck, C.4    Regnier, F.E.5    Zhang, X.6
  • 32
    • 76149132007 scopus 로고    scopus 로고
    • Comparison of Database Search Strategies for High Precursor Mass Accuracy MS/MS Data
    • Hsieh, E. J.; Hoopmann, M. R.; MacLean, B.; MacCoss, M. J. Comparison of Database Search Strategies for High Precursor Mass Accuracy MS/MS Data J. Proteome Res. 2010, 9 (2) 1138-1143
    • (2010) J. Proteome Res. , vol.9 , Issue.2 , pp. 1138-1143
    • Hsieh, E.J.1    Hoopmann, M.R.2    MacLean, B.3    MacCoss, M.J.4
  • 33
    • 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. A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data BMC Bioinform. 2007, 8, 133
    • (2007) BMC Bioinform. , vol.8 , pp. 133
    • Xu, H.1    Freitas, M.A.2
  • 34
    • 57449099068 scopus 로고    scopus 로고
    • Precision proteomics: The case for high resolution andhigh mass accuracy
    • Mann, M.; Kelleher, N. L. Precision proteomics: The case for high resolution andhigh mass accuracy Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 18132-18138
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18132-18138
    • Mann, M.1    Kelleher, N.L.2
  • 35
    • 72149119458 scopus 로고    scopus 로고
    • Multidimensional protein fractionation of blood proteins coupled to data-independent nanoLC-MS/MS analysis
    • Levin, Y.; Jaros, J. A.; Schwarz, E.; Bahn, S. Multidimensional protein fractionation of blood proteins coupled to data-independent nanoLC-MS/MS analysis J. Protoemics 2010, 73 (3) 689-695
    • (2010) J. Protoemics , vol.73 , Issue.3 , pp. 689-695
    • Levin, Y.1    Jaros, J.A.2    Schwarz, E.3    Bahn, S.4
  • 36
    • 77954365852 scopus 로고    scopus 로고
    • Improving Protein and Proteome Coverage through Data-Independent Multiplexed Peptide Fragmentation
    • Blackburn, K.; Mbeunkui, F.; Mitra, S. K.; Mentzel, T.; Goshe, M. B. Improving Protein and Proteome Coverage through Data-Independent Multiplexed Peptide Fragmentation J. Proteome Res. 2010, 9 (7) 3621-3637
    • (2010) J. Proteome Res. , vol.9 , Issue.7 , pp. 3621-3637
    • Blackburn, K.1    Mbeunkui, F.2    Mitra, S.K.3    Mentzel, T.4    Goshe, M.B.5
  • 37
    • 16644396658 scopus 로고    scopus 로고
    • Intrinsic Amino Acid Size Parameters from a Series of 113 Lysine-Terminated Tryptic Digest Peptide Ions
    • Valentine, S. J.; Counterman, A. E.; Hoaglund-Hyzer, C. S.; Clemmer, D. E. Intrinsic Amino Acid Size Parameters from a Series of 113 Lysine-Terminated Tryptic Digest Peptide Ions J. Phys. Chem. B 1999, 103, 1203-1207
    • (1999) J. Phys. Chem. B , vol.103 , pp. 1203-1207
    • Valentine, S.J.1    Counterman, A.E.2    Hoaglund-Hyzer, C.S.3    Clemmer, D.E.4
  • 38
    • 0001070559 scopus 로고    scopus 로고
    • Intrinsic Size Parameters for Val, Ile, Leu, Gln, Thr, Phe, and Trp Residues from Ion Mobility Measurements of Polyamino Acid Ions
    • Henderson, S. C.; Li, J.; Counterman, A. E.; Clemmer, D. E. Intrinsic Size Parameters for Val, Ile, Leu, Gln, Thr, Phe, and Trp Residues from Ion Mobility Measurements of Polyamino Acid Ions J. Phys. Chem. B 1999, 103, 8780-8785 (Pubitemid 129613923)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.41 , pp. 8780-8785
    • Henderson, S.C.1    Li, J.2    Counterman, A.E.3    Clemmer, D.E.4
  • 39
    • 0033473749 scopus 로고    scopus 로고
    • A database of 660 peptide ion cross sections: Use of intrinsic size parameters for bona fide predictions of cross sections
    • DOI 10.1016/S1044-0305(99)00079-3, PII S1044030599000793
    • Valentine, S. J.; Counterman, A. E.; Clemmer, D. E. A Database of 660 Peptide Ion Cross Sections: Use of Intrinsic Size Parameters for Bona Fide Predictions of Cross Sections J. Am. Soc. Mass Spectrom. 1999, 10, 1188-1211 (Pubitemid 34498675)
    • (1999) Journal of the American Society for Mass Spectrometry , vol.10 , Issue.11 , pp. 1188-1211
    • Valentine, S.J.1    Counterman, A.E.2    Clemmer, D.E.3
  • 40
    • 0033611971 scopus 로고    scopus 로고
    • Volumes of Individual Amino Acid Residues in Gas-Phase Peptide Ions
    • Counterman, A. E.; Clemmer, D. E. Volumes of Individual Amino Acid Residues in Gas-Phase Peptide Ions J. Am. Chem. Soc. 1999, 121, 4031-4039
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4031-4039
    • Counterman, A.E.1    Clemmer, D.E.2
  • 41
    • 77950664005 scopus 로고    scopus 로고
    • Artificial neural networks for the prediction of peptide drift time in ion mobility mass spectrometry
    • Wang, B.; Valentine, S.; Plasencia, M.; Raghuraman, S.; Zhang, X. Artificial neural networks for the prediction of peptide drift time in ion mobility mass spectrometry BMC Bioinform. 2010, 11, 182
    • (2010) BMC Bioinform. , vol.11 , pp. 182
    • Wang, B.1    Valentine, S.2    Plasencia, M.3    Raghuraman, S.4    Zhang, X.5
  • 42
    • 80051751860 scopus 로고
    • Ion Mobility Spectrometry in Analytical Chemistry
    • For a review of IMS techniques see (and references therein)
    • For a review of IMS techniques see (and references therein): St. Louis, R. H.; Hill, H. H. Ion Mobility Spectrometry in Analytical Chemistry Crit. Rev. Anal. Chem. 1990, 21, 321-355
    • (1990) Crit. Rev. Anal. Chem. , vol.21 , pp. 321-355
    • St. Louis, R.H.1    Hill, H.H.2
  • 43
    • 0030905633 scopus 로고    scopus 로고
    • Ion mobility measurements and their applications to clusters and biomolecules
    • DOI 10.1002/(SICI)1096-9888(19 9706)32:6<577::AID-JMS530>3.0.CO;2-4
    • For a review of IMS techniques see (and references therein): Clemmer, D. E.; Jarrold, M. F. Ion Mobility Measurements and their Applications to Clusters and Biomolecules J. Mass Spectrom. 1997, 32, 577-592 (Pubitemid 27273948)
    • (1997) Journal of Mass Spectrometry , vol.32 , Issue.6 , pp. 577-592
    • Clemmer, D.E.1    Jarrold, M.F.2
  • 44
    • 15144345257 scopus 로고    scopus 로고
    • Characterizing Oligosaccharides Using Injected-Ion Mobility/Mass Spectrometry
    • Liu, Y.; Clemmer, D. E. Characterizing Oligosaccharides Using Injected-Ion Mobility/Mass Spectrometry Anal. Chem. 1997, 69, 2504-2509
    • (1997) Anal. Chem. , vol.69 , pp. 2504-2509
    • Liu, Y.1    Clemmer, D.E.2
  • 46
    • 57449100366 scopus 로고    scopus 로고
    • Biomolecule Analysis by Ion Mobility Spectrometry
    • For a review of IMS techniques see (and references therein):;;;;, ()
    • For a review of IMS techniques see (and references therein): Bohrer, B. C.; Merenbloom, S. I.; Koeniger, S. L.; Hilderbrand, A. E.; Clemmer, D. E. Biomolecule Analysis by Ion Mobility Spectrometry Annu. Rev. Anal. Chem. 2008, 1 (10) 1-10
    • (2008) Annu. Rev. Anal. Chem. , vol.1 , Issue.10 , pp. 1-10
    • Bohrer, B.C.1    Merenbloom, S.I.2    Koeniger, S.L.3    Hilderbrand, A.E.4    Clemmer, D.E.5
  • 47
    • 0001015266 scopus 로고
    • Electrospray Ionization Ion Mobility Spectrometry
    • Wittmer, D.; Luckenbill, B. K.; Hill, H. H.; Chen, Y. H. Electrospray Ionization Ion Mobility Spectrometry Anal. Chem. 1994, 66, 2348-2355
    • (1994) Anal. Chem. , vol.66 , pp. 2348-2355
    • Wittmer, D.1    Luckenbill, B.K.2    Hill, H.H.3    Chen, Y.H.4
  • 49
    • 0034282963 scopus 로고    scopus 로고
    • Coupling High-Pressure MALDI with Ion Mobility/Orthogonal Time-of Flight Mass Spectrometry
    • Gillig, K. J.; Ruotolo, B.; Stone, E. G.; Russell, D. H.; Fuhrer, K.; Gonin, M.; Schultz, A. J. Coupling High-Pressure MALDI with Ion Mobility/Orthogonal Time-of Flight Mass Spectrometry Anal. Chem. 2000, 72, 3965-3971
    • (2000) Anal. Chem. , vol.72 , pp. 3965-3971
    • Gillig, K.J.1    Ruotolo, B.2    Stone, E.G.3    Russell, D.H.4    Fuhrer, K.5    Gonin, M.6    Schultz, A.J.7
  • 50
    • 0034234619 scopus 로고    scopus 로고
    • Mobility labeling for parallel CID of ion mixtures
    • DOI 10.1021/ac0000170
    • Hoaglund-Hyzer, C. S.; Li, J.; Clemmer, D. E. Mobility Labeling for Parallel CID of Ion Mixtures Anal. Chem. 2000, 72, 2737-2740 (Pubitemid 30452237)
    • (2000) Analytical Chemistry , vol.72 , Issue.13 , pp. 2737-2740
    • Hoaglund-Hyzer, C.S.1    Li, J.2    Clemmer, D.E.3
  • 51
    • 0035863707 scopus 로고    scopus 로고
    • Ion trap/ion mobility/quadrupole/time-of-flight mass spectrometry for peptide mixture analysis
    • DOI 10.1021/ac0007783
    • Hoaglund-Hyzer, C. S.; Clemmer, D. E. Ion Trap/Ion Mobility/Quadrupole/ Time-of-Flight Mass Spectrometry for Peptide Mixture Analysis Anal. Chem. 2001, 73, 177-184 (Pubitemid 32061826)
    • (2001) Analytical Chemistry , vol.73 , Issue.2 , pp. 177-184
    • Hoaglund-Hyzer, C.S.1    Clemmer, D.E.2
  • 52
    • 0036500991 scopus 로고    scopus 로고
    • Coupling ion mobility separations, collisional activation techniques, and multiple stages of MS for analysis of complex peptide mixtures
    • DOI 10.1021/ac010837s
    • Hoaglund-Hyzer, C. S.; Lee, Y. J.; Counterman, A. E.; Clemmer, D. E. Coupling Ion Mobility Separations, Collisional Activation Techniques, and Multiple Stages of MS for Analysis of Complex Peptide Mixtures Anal. Chem. 2002, 74, 992-1006 (Pubitemid 34203021)
    • (2002) Analytical Chemistry , vol.74 , Issue.5 , pp. 992-1006
    • Hoaglund-Hyzer, C.S.1    Lee, Y.J.2    Counterman, A.E.3    Clemmer, D.E.4
  • 55
    • 0016520487 scopus 로고
    • Theory of Plasma Chromatography Gaseous Electrophoresis - Review
    • Revercomb, H. E.; Mason, E. A. Theory of Plasma Chromatography Gaseous Electrophoresis-Review Anal. Chem. 1975, 47, 970-983
    • (1975) Anal. Chem. , vol.47 , pp. 970-983
    • Revercomb, H.E.1    Mason, E.A.2
  • 57
    • 0030580028 scopus 로고    scopus 로고
    • An exact hard-spheres scattering model for the mobilities of polyatomic ions
    • PII S0009261496009414
    • Shvartsburg, A. A.; Jarrold, M. F. An exact hard-spheres scattering model for the mobilities of polyatomic ions Chem. Phys. Lett. 1996, 261, 86-91 (Pubitemid 126163393)
    • (1996) Chemical Physics Letters , vol.261 , Issue.1-2 , pp. 86-91
    • Shvartsburg, A.A.1    Jarrold, M.F.2
  • 58
    • 33748887803 scopus 로고    scopus 로고
    • Structural information from ion mobility measurements: Effects of the long-range potential
    • Mesleh, M. F.; Hunter, J. M.; Shvartsburg, A. A.; Schatz, G. C.; Jarrold, M. F. Structural information from ion mobility measurements: effects of the long-range potential J. Phys. Chem. 1996, 100, 16082-16086 (Pubitemid 126799343)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.40 , pp. 16082-16086
    • Mesleh, M.F.1    Hunter, J.M.2    Shvartsburg, A.A.3    Schatz, G.C.4    Jarrold, M.F.5
  • 60
    • 0035891934 scopus 로고    scopus 로고
    • Multidimensional separations of complex peptide mixtures: A combined high-performance liquid chromatography/ion mobility/time-of-flight mass spectrometry approach
    • Valentine, S. J.; Kulchania, M.; Srebalus Barnes, C. A.; Clemmer, D. E. Multidimensional separations of complex peptide mixtures: a combined high-performance liquid chromatography/ion mobility/time-of-flight mass spectrometry approach Int. J. Mass Spectrom. 2001, 212, 97-109
    • (2001) Int. J. Mass Spectrom. , vol.212 , pp. 97-109
    • Valentine, S.J.1    Kulchania, M.2    Srebalus Barnes, C.A.3    Clemmer, D.E.4
  • 61
    • 0036139784 scopus 로고    scopus 로고
    • Resolving isomeric peptide mixtures: A combined HPLC/ion mobility-TOFMS analysis of a 4000-component combinatorial library
    • DOI 10.1021/ac0108562
    • Srebalus Barnes, C. A.; Hilderbrand, A. E.; Valentine, S. J.; Clemmer, D. E. Resolving Isomeric Peptide Mixtures: A Combined HPLC/Ion Mobility-TOFMS Analysis of a 4000-Component Combinatorial Library Anal. Chem. 2002, 74, 26-36 (Pubitemid 34044420)
    • (2002) Analytical Chemistry , vol.74 , Issue.1 , pp. 26-36
    • Srebalus Barnes, C.A.1    Hilderbrand, A.E.2    Valentine, S.J.3    Clemmer, D.E.4
  • 62
    • 0348142994 scopus 로고    scopus 로고
    • Nanoflow LC/Ion Mobility/CID/TOF for Proteomics: Analysis of a Human Urinary Proteome
    • DOI 10.1021/pr034018v
    • Moon, M. H.; Myung, S.; Plasencia, M.; Hilderbrand, A. E.; Clemmer, D. E. Nanoflow LC/Ion Mobility/CID/TOF for Proteomics: Analysis of a Human Urinary Proteome J. Proteome Res. 2003, 2, 589-597 (Pubitemid 38017103)
    • (2003) Journal of Proteome Research , vol.2 , Issue.6 , pp. 589-597
    • Moon, M.H.1    Myung, S.2    Plasencia, M.3    Hilderbrand, A.E.4    Clemmer, D.E.5
  • 67
    • 79955794619 scopus 로고    scopus 로고
    • The Mathworks, Inc.
    • The Mathworks, Inc. http://www.mathworks.com/products/matlab/.
  • 69
    • 79955795535 scopus 로고    scopus 로고
    • http://en.wikipedia.org/wiki/Numerical-methods-for-linear-least-squares.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.