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Volumn 21, Issue 8, 2010, Pages 1339-1351

'Fixed charge' chemical derivatization and data dependant multistage tandem mass spectrometry for mapping protein surface residue accessibility

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINS; CHEMICAL ANALYSIS; CHEMICAL REACTIONS; IONS; MAPPING; MASS SPECTROMETERS; MASS SPECTROMETRY; PEPTIDES; PROTEINS;

EID: 77958185973     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1016/j.jasms.2010.03.047     Document Type: Article
Times cited : (21)

References (43)
  • 1
    • 34547640455 scopus 로고    scopus 로고
    • Mass spectrometry-based approaches for structural studies on protein complexes at low-resolution
    • Renzone, G.; Salzano, A. M.; Arena, S.; Ambrosio, C. D.; Scaloni, A. Mass Spectrometry-Based Approaches for Structural Studies on Protein Complexes at Low-Resolution. Curr. Proteom. 2007, 4, 1-16.
    • (2007) Curr. Proteom. , vol.4 , pp. 1-16
    • Renzone, G.1    Salzano, A.M.2    Arena, S.3    Ambrosio, C.D.4    Scaloni, A.5
  • 2
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • Englander, S. W. Hydrogen Exchange and Mass Spectrometry: A Historical Perspective. J. Am. Soc. Mass Spectrom. 2006, 17, 1481-1489.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1481-1489
    • Englander, S.W.1
  • 3
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales, T. E.; Engen, J. R. Hydrogen Exchange Mass Spectrometry for the Analysis of Protein Dynamics. Mass Spectrom. Rev. 2006, 25, 158-170.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 4
    • 34548337296 scopus 로고    scopus 로고
    • Hydroxyl radical-mediated modification of proteins as probes for structural proteomics
    • Xu, G.; Chance, M. R. Hydroxyl Radical-Mediated Modification of Proteins as Probes for Structural Proteomics. Chem. Rev. 2007, 107, 3514-3543.
    • (2007) Chem. Rev. , vol.107 , pp. 3514-3543
    • Xu, G.1    Chance, M.R.2
  • 5
    • 77955671120 scopus 로고    scopus 로고
    • Mass spectrometry combined with oxidative labeling for exploring protein structure and folding
    • in press. DOI: 10.1002/mas.20256
    • Konermann, L.; Stocks, B. B.; Pan, Y.; Tong, X. Mass Spectrometry Combined with Oxidative Labeling for Exploring Protein Structure and Folding. Mass Spectrom. Rev. 2010, in press. DOI: 10.1002/mas.20256.
    • (2010) Mass Spectrom. Rev.
    • Konermann, L.1    Stocks, B.B.2    Pan, Y.3    Tong, X.4
  • 6
    • 69849100869 scopus 로고    scopus 로고
    • Probing protein structure by amino acid-specific covalent labeling and mass spectrometry
    • Mendoza, V. L.; Vachet, R. W. Probing Protein Structure by Amino Acid-Specific Covalent Labeling and Mass Spectrometry. Mass Spectrom. Rev. 2009, 28, 785-815.
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 785-815
    • Mendoza, V.L.1    Vachet, R.W.2
  • 7
    • 70349632883 scopus 로고    scopus 로고
    • H/D exchange and mass spectrometry in the studies of protein conformation and dynamics: Is there a need for a top-down approach?
    • Kaltashov, I. A.; Bobst, C. E.; Abzalimov, R. R. H/D Exchange and Mass Spectrometry in the Studies of Protein Conformation and Dynamics: Is There a Need for a Top-Down Approach? Anal. Chem. 2009, 81, 7892-7899.
    • (2009) Anal. Chem. , vol.81 , pp. 7892-7899
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3
  • 8
    • 60649094922 scopus 로고    scopus 로고
    • Fast reversed-phase liquid chromatography to reduce back-exchange and increase throughput in H/D exchange monitored by FT-ICR mass spectrometry
    • Zhang, H. M.; Bou-Assaf, G. M.; Emmett, M. R.; Marshall, A. G. Fast Reversed-Phase Liquid Chromatography to Reduce Back-Exchange and Increase Throughput in H/D Exchange Monitored by FT-ICR Mass Spectrometry. J. Am. Soc. Mass Spectrom. 2009, 20, 520-524.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 520-524
    • Zhang, H.M.1    Bou-Assaf, G.M.2    Emmett, M.R.3    Marshall, A.G.4
  • 9
    • 14744272834 scopus 로고    scopus 로고
    • Intramolecular migration of amide hydrogens in protonated peptides upon collisional activation
    • Jorgensen, T. J. D.; Gardsvoll, H.; Ploug, M.; Roepstorff, P. Intramolecular Migration of Amide Hydrogens in Protonated Peptides upon Collisional Activation. J. Am. Chem. Soc. 2005, 127, 2785-2793.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2785-2793
    • Jorgensen, T.J.D.1    Gardsvoll, H.2    Ploug, M.3    Roepstorff, P.4
  • 10
    • 67650756766 scopus 로고    scopus 로고
    • Protein hydrogen exchange measured at single-residue resolution by electron transfer dissociation mass spectrometry
    • Rand, K. D.; Zehl, M.; Jensen, O. N.; Jorgensen, T. J. D. Protein Hydrogen Exchange Measured at Single-Residue Resolution by Electron Transfer Dissociation Mass Spectrometry. Anal. Chem. 2009, 81, 5577-5584.
    • (2009) Anal. Chem. , vol.81 , pp. 5577-5584
    • Rand, K.D.1    Zehl, M.2    Jensen, O.N.3    Jorgensen, T.J.D.4
  • 11
    • 38649092998 scopus 로고    scopus 로고
    • Electron capture dissociation proceeds with a low degree of intramolecular migration of peptide amide hydrogens
    • Rand, K. D.; Adams, C. M.; Zubarev, R. A.; Jorgensen, T. J. D. Electron Capture Dissociation Proceeds with a Low Degree of Intramolecular Migration of Peptide Amide Hydrogens. J. Am. Chem. Soc. 2008, 130, 1341-1349.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1341-1349
    • Rand, K.D.1    Adams, C.M.2    Zubarev, R.A.3    Jorgensen, T.J.D.4
  • 12
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions
    • Sinz, A. Chemical Cross-Linking and Mass Spectrometry to Map Three-Dimensional Protein Structures and Protein-Protein Interactions. Mass Spectrom. Rev. 2006, 25, 663-682.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 663-682
    • Sinz, A.1
  • 13
    • 25144465204 scopus 로고    scopus 로고
    • Radiolytic modification and reactivity of amino acid residues serving as structural probes for protein footprinting
    • Xu, G.; Chance, M. R. Radiolytic Modification and Reactivity of Amino Acid Residues Serving as Structural Probes for Protein Footprinting. Anal. Chem. 2005, 77, 4549-4555.
    • (2005) Anal. Chem. , vol.77 , pp. 4549-4555
    • Xu, G.1    Chance, M.R.2
  • 14
    • 0037035538 scopus 로고    scopus 로고
    • Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting
    • Guan, J. Q.; Vorobiev, S.; Almo, S. C.; Chance, M. R. Mapping the G-Actin Binding Surface of Cofilin Using Synchrotron Protein Footprinting. Biochemistry 2002, 41, 5765-5775.
    • (2002) Biochemistry , vol.41 , pp. 5765-5775
    • Guan, J.Q.1    Vorobiev, S.2    Almo, S.C.3    Chance, M.R.4
  • 15
    • 33646864750 scopus 로고    scopus 로고
    • Measurement of multisite oxidation kinetics reveals an active site conformational change in Spo0F as a result of protein oxidation
    • Sharp, J. S.; Sullivan, D. M.; Cavanagh, J.; Tomer, K. B. Measurement of Multisite Oxidation Kinetics Reveals an Active Site Conformational Change in Spo0F as a Result of Protein Oxidation. Biochemistry 2006, 45, 6260-6266.
    • (2006) Biochemistry , vol.45 , pp. 6260-6266
    • Sharp, J.S.1    Sullivan, D.M.2    Cavanagh, J.3    Tomer, K.B.4
  • 16
    • 33746260405 scopus 로고    scopus 로고
    • Effects of anion proximity in peptide primary sequence on the rate and mechanism of leucine oxidation
    • Sharp, J. S.; Tomer, K. B. Effects of Anion Proximity in Peptide Primary Sequence on the Rate and Mechanism of Leucine Oxidation. Anal. Chem. 2006, 78, 4885-4893.
    • (2006) Anal. Chem. , vol.78 , pp. 4885-4893
    • Sharp, J.S.1    Tomer, K.B.2
  • 17
    • 33847794081 scopus 로고    scopus 로고
    • Analysis of the oxidative damage-induced conformational changes of apo- and holocalmodulin by dose-dependent protein oxidative surface mapping
    • Sharp, J. S.; Tomer, K. B. Analysis of the Oxidative Damage-Induced Conformational Changes of Apo- and Holocalmodulin by Dose-Dependent Protein Oxidative Surface Mapping. Biophys. J. 2007, 92, 1682-1692.
    • (2007) Biophys. J. , vol.92 , pp. 1682-1692
    • Sharp, J.S.1    Tomer, K.B.2
  • 18
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping
    • Suckau, D.; Mak, M.; Przybylski, M. Protein Surface Topology-Probing by Selective Chemical Modification and Mass Spectrometric Peptide Mapping. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 5630-5634.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 20
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein- protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai, C. J.; Lin, S. L.; Wolfson, H. J.; Nussinov, R. Studies of Protein- Protein Interfaces: A Statistical Analysis of the Hydrophobic Effect. Protein Sci. 1997, 6, 53-64.
    • (1997) Protein Sci. , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 21
    • 33751010168 scopus 로고    scopus 로고
    • Probing the structure of the caulobacter crescentus ribosome with chemical labeling and mass spectrometry
    • Beardsley, R. L.; Running, W. E.; Reilly, J. P. Probing the Structure of the Caulobacter crescentus Ribosome with Chemical Labeling and Mass Spectrometry. J. Proteome Res. 2006, 5, 2935-2946.
    • (2006) J. Proteome Res. , vol.5 , pp. 2935-2946
    • Beardsley, R.L.1    Running, W.E.2    Reilly, J.P.3
  • 22
    • 33745260411 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction surfaces using a combination of efficient lysine acetylation and nanoLC-MALDI-MS/MS applied to the E9:Im9 bacteriotoxin-immunity protein complex
    • Scholten, A.; Visser, N. F. C.; van den Heuvel R. H. H.; Heck, A. J. R. Analysis of Protein-Protein Interaction Surfaces Using a Combination of Efficient Lysine Acetylation and nanoLC-MALDI-MS/MS Applied to the E9:Im9 Bacteriotoxin-Immunity Protein Complex. J. Am. Soc. Mass Spectrom. 2006, 17, 983-994.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 983-994
    • Scholten, A.1    Visser, N.F.C.2    Van Den Heuvel, R.H.H.3    Heck, A.J.R.4
  • 23
    • 64649085349 scopus 로고    scopus 로고
    • Mass spectrometry-based footprinting of protein-protein interactions
    • McKee, C. J.; Kessl, J. J.; Norris, J. O.; Shkriabai, N.; Kvaratskhelia, M. Mass Spectrometry-Based Footprinting of Protein-Protein Interactions. Methods 2009, 47, 304-307.
    • (2009) Methods , vol.47 , pp. 304-307
    • McKee, C.J.1    Kessl, J.J.2    Norris, J.O.3    Shkriabai, N.4    Kvaratskhelia, M.5
  • 24
    • 12344283723 scopus 로고    scopus 로고
    • Mass spectrometric identification of lysines involved in the interaction of human replication protein a with single-stranded DNA
    • Shell, S. M.; Hess, S.; Kvaratskhelia, M.; Zou, Y. Mass Spectrometric Identification of Lysines Involved in the Interaction of Human Replication Protein A with Single-Stranded DNA. Biochemistry 2005, 44, 971-978.
    • (2005) Biochemistry , vol.44 , pp. 971-978
    • Shell, S.M.1    Hess, S.2    Kvaratskhelia, M.3    Zou, Y.4
  • 25
    • 1642368829 scopus 로고    scopus 로고
    • A top-down method for the determination of residue-specific solvent accessibility in proteins
    • Novak, P.; Kruppa, G. H.; Young, M. M.; Schoeniger, J. A Top-Down Method for the Determination of Residue-Specific Solvent Accessibility in Proteins. J. Mass Spectrom. 2004, 39, 322-328.
    • (2004) J. Mass Spectrom. , vol.39 , pp. 322-328
    • Novak, P.1    Kruppa, G.H.2    Young, M.M.3    Schoeniger, J.4
  • 26
    • 27144451208 scopus 로고    scopus 로고
    • Probing the ligand-induced conformational change in HLA-DR1 by selective chemical modification and mass spectrometric mapping
    • Carven, G. J.; Stern, L. J. Probing the Ligand-Induced Conformational Change in HLA-DR1 by Selective Chemical Modification and Mass Spectrometric Mapping. Biochemistry 2005, 44, 13625-13637.
    • (2005) Biochemistry , vol.44 , pp. 13625-13637
    • Carven, G.J.1    Stern, L.J.2
  • 27
    • 27944463670 scopus 로고    scopus 로고
    • Probing protein tertiary structure with amidination
    • Janecki, D. J.; Beardsley, R. L.; Reilly, J. P. Probing Protein Tertiary Structure with Amidination. Anal. Chem. 2005, 77, 7274-7281.
    • (2005) Anal. Chem. , vol.77 , pp. 7274-7281
    • Janecki, D.J.1    Beardsley, R.L.2    Reilly, J.P.3
  • 28
    • 20444490423 scopus 로고    scopus 로고
    • Selective identification and quantitative analysis of methionine containing peptides by charge derivatization and tandem mass spectrometry
    • Reid, G. E.; Roberts, K. D.; Simpson, R. J.; O'Hair, R. A. J. Selective Identification and Quantitative Analysis of Methionine Containing Peptides by Charge Derivatization and Tandem Mass Spectrometry. J. Am. Soc. Mass Spectrom. 2005, 16, 1131-1150.
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 1131-1150
    • Reid, G.E.1    Roberts, K.D.2    Simpson, R.J.3    O'hair, R.A.J.4
  • 29
    • 33751333714 scopus 로고    scopus 로고
    • Mechanisms for the selective gas-phase fragmentation reactions of methionine side chain fixed charge sulfonium ion containing peptides
    • Amunugama, M.; Roberts, K. D.; Reid, G. E. Mechanisms for the Selective Gas-Phase Fragmentation Reactions of Methionine Side Chain Fixed Charge Sulfonium Ion Containing Peptides. J. Am. Soc. Mass Spectrom. 2006, 17, 1631-1642.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1631-1642
    • Amunugama, M.1    Roberts, K.D.2    Reid, G.E.3
  • 30
    • 33947729657 scopus 로고    scopus 로고
    • Substituent effects on the gas-phase fragmentation reactions of sulfonium ion containing peptides
    • Sierakowski, J.; Amunugama, M.; Roberts, K. D.; Reid, G. E. Substituent Effects on the Gas-Phase Fragmentation Reactions of Sulfonium Ion Containing Peptides. Rapid Commun. Mass Spectrom. 2007, 21, 1230-1238.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 1230-1238
    • Sierakowski, J.1    Amunugama, M.2    Roberts, K.D.3    Reid, G.E.4
  • 31
    • 53549129478 scopus 로고    scopus 로고
    • Automated neutral loss and data dependent energy resolved "pseudo MS3" for the targeted identification, characterization and quantitative analysis of methionine- containing peptides
    • Froelich, J. M.; Kaplinghat, S.; Reid, G. E. Automated Neutral Loss and Data Dependent Energy Resolved "pseudo MS3" for the Targeted Identification, Characterization and Quantitative Analysis of Methionine- Containing Peptides. Eur. J. Mass Spectrom. 2008, 14, 219-299.
    • (2008) Eur. J. Mass Spectrom. , vol.14 , pp. 219-299
    • Froelich, J.M.1    Kaplinghat, S.2    Reid, G.E.3
  • 32
    • 33847075498 scopus 로고    scopus 로고
    • Leaving group effects on the selectivity of the gas-phase fragmentation reactions of side chain fixed-charge-containing peptide ions
    • Roberts, K. D.; Reid, G. E. Leaving Group Effects on the Selectivity of the Gas-Phase Fragmentation Reactions of Side Chain Fixed-Charge-Containing Peptide Ions. J. Mass Spectrom. 2007, 42, 187-198.
    • (2007) J. Mass Spectrom. , vol.42 , pp. 187-198
    • Roberts, K.D.1    Reid, G.E.2
  • 33
    • 57449117894 scopus 로고    scopus 로고
    • Ionic reagent for controlling the gas-phase fragmentation reactions of cross-linked peptides
    • Lu, Y.; Tanasova, M.; Borhan, B.; Reid, G. E. Ionic Reagent for Controlling the Gas-Phase Fragmentation Reactions of Cross-Linked Peptides. Anal. Chem. 2008, 80, 9279-9287.
    • (2008) Anal. Chem. , vol.80 , pp. 9279-9287
    • Lu, Y.1    Tanasova, M.2    Borhan, B.3    Reid, G.E.4
  • 34
    • 0034501099 scopus 로고    scopus 로고
    • Mobile and localized protons: A framework for understanding peptide dissociation
    • Wysocki, V. H.; Tsaprailis, G.; Smith, L. L.; Breci, L. A. Mobile and Localized Protons: A Framework for Understanding Peptide Dissociation. J. Mass Spectrom. 2000, 35, 1399-1406.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 1399-1406
    • Wysocki, V.H.1    Tsaprailis, G.2    Smith, L.L.3    Breci, L.A.4
  • 35
    • 0029810698 scopus 로고    scopus 로고
    • Influence of peptide composition, gas-phase basicity, and chemical modification on fragmentation efficiency: Evidence for the mobile proton model
    • Dongre, A. R.; Jones, J. L.; Somogyi, A.; Wysocki, V. H. Influence of Peptide Composition, Gas-Phase Basicity, and Chemical Modification on Fragmentation Efficiency: Evidence for the Mobile Proton Model. J. Am. Chem. Soc. 1996, 118, 8365-8374.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8365-8374
    • Dongre, A.R.1    Jones, J.L.2    Somogyi, A.3    Wysocki, V.H.4
  • 36
    • 0030000913 scopus 로고    scopus 로고
    • Role of the site of protonation in the low-energy decompositions of gas-phase peptide ions
    • Cox, K. A.; Gaskell, S. J.; Morris, M.; Whiting, A. Role of the Site of Protonation in the Low-Energy Decompositions of Gas-Phase Peptide Ions. J. Am. Soc. Mass Spectrom. 1996, 7, 522-531.
    • (1996) J. Am. Soc. Mass Spectrom. , vol.7 , pp. 522-531
    • Cox, K.A.1    Gaskell, S.J.2    Morris, M.3    Whiting, A.4
  • 37
    • 0242653718 scopus 로고    scopus 로고
    • Mining a tandem mass spectrometry database to determine the trends and global factors influencing peptide fragmentation
    • Kapp, E. A.; Schu1tz, F.; Reid, G. E.; Eddes, J. S.; Moritz, R. L.; O'Hair, R. A. J.; Speed, T. P.; Simpson, R. J. Mining a Tandem Mass Spectrometry Database to Determine the Trends and Global Factors Influencing Peptide Fragmentation. Anal. Chem. 2003, 75, 6251-6264.
    • (2003) Anal. Chem. , vol.75 , pp. 6251-6264
    • Kapp, E.A.1    Schultz, F.2    Reid, G.E.3    Eddes, J.S.4    Moritz, R.L.5    O'hair, R.A.J.6    Speed, T.P.7    Simpson, R.J.8
  • 38
    • 0032530468 scopus 로고    scopus 로고
    • Solution structure of type II human cellular retinoic acid binding protein: Implications for ligand binding
    • Wang, L.; Li, Y.; Abildgaard, F.; Markley, J. L.; Yan, H. NMR. Solution Structure of Type II Human Cellular Retinoic Acid Binding Protein: Implications for Ligand Binding. Biochemistry 1998, 37, 12727-12736.
    • (1998) Biochemistry , vol.37 , pp. 12727-12736
    • Wang, L.1    Li, Y.2    Abildgaard, F.3    Markley, J.L.4    Yan, H.N.M.R.5
  • 39
    • 33845378608 scopus 로고
    • Neighboring-group participation in organic redox reactions. 10. The kinetic and mechanistic effects of imidazole and benzimidazole nitrogen on thioether oxidations
    • Williams, K. A; Doi, J. T; Musker, W. K. Neighboring-Group Participation in Organic Redox Reactions. 10. The Kinetic and Mechanistic Effects of Imidazole and Benzimidazole Nitrogen on Thioether Oxidations. J. Org. Chem. 1985, 50, 4-10.
    • (1985) J. Org. Chem. , vol.50 , pp. 4-10
    • Williams, K.A.1    Doi, J.T.2    Musker, W.K.3
  • 40
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R.; Braun, W. Exact and Efficient Analytical Calculation of the Accessible Surface Areas and Their Gradients for Macromolecules. J. Comput. Chem. 1998, 19, 319-333.
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 42
    • 34648828201 scopus 로고    scopus 로고
    • Experimental and theoretical proton affinities of methionine, methionine sulfoxide, and their N- and C-terminal derivatives
    • Lioe, H.; O'Hair, R. A. J.; Gronert, S.; Austin, A.; Reid, G. E. Experimental and Theoretical Proton Affinities of Methionine, Methionine Sulfoxide, and their N- and C-Terminal Derivatives. Int. J. Mass Spectrom. 2007, 267, 220-232.
    • (2007) Int. J. Mass Spectrom. , vol.267 , pp. 220-232
    • Lioe, H.1    O'hair, R.A.J.2    Gronert, S.3    Austin, A.4    Reid, G.E.5
  • 43
    • 3543043134 scopus 로고    scopus 로고
    • Enrichment of cysteine-containing peptides from tryptic digests using a quaternary amine tag
    • Ren, D.; Julka, S.; Inerowicz, H. D.; Regnier, F. E. Enrichment of Cysteine-Containing Peptides from Tryptic Digests Using a Quaternary Amine Tag. Anal. Chem. 2004, 76, 4522-4530.
    • (2004) Anal. Chem. , vol.76 , pp. 4522-4530
    • Ren, D.1    Julka, S.2    Inerowicz, H.D.3    Regnier, F.E.4


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