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Volumn 85, Issue 19, 2013, Pages 9173-9180

A new approach to measuring protein backbone protection with high spatial resolution using H/D exchange and electron capture dissociation

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL DYNAMICS; ELECTRON CAPTURE DISSOCIATION; HIGH SPATIAL RESOLUTION; HUMAN SERUM TRANSFERRIN; HYDROGEN SCRAMBLING; ION FRAGMENTATION; MODE OF OPERATIONS; SPATIAL RESOLUTION;

EID: 84884996292     PISSN: 00032700     EISSN: 15206882     Source Type: Journal    
DOI: 10.1021/ac401868b     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • Engen, J. R. Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS Anal. Chem. 2009, 81, 7870-7875
    • (2009) Anal. Chem. , vol.81 , pp. 7870-7875
    • Engen, J.R.1
  • 2
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann, L.; Pan, J.; Liu, Y.-H. Hydrogen exchange mass spectrometry for studying protein structure and dynamics Chem. Soc. Rev. 2011, 40, 1224-1234
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.-H.3
  • 4
    • 84878285699 scopus 로고    scopus 로고
    • Mass spectrometry-based methods to study protein architecture and dynamics
    • Kaltashov, I. A.; Bobst, C. E.; Abzalimov, R. R. Mass spectrometry-based methods to study protein architecture and dynamics Protein Sci. 2013, 22, 530-544
    • (2013) Protein Sci. , vol.22 , pp. 530-544
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3
  • 5
    • 0030027339 scopus 로고    scopus 로고
    • Investigation of protein folding by mass spectrometry
    • Miranker, A.; Robinson, C. V.; Radford, S. E.; Dobson, C. M. Investigation of protein folding by mass spectrometry FASEB J. 1996, 10, 93-101
    • (1996) FASEB J. , vol.10 , pp. 93-101
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Dobson, C.M.4
  • 6
    • 35648957285 scopus 로고    scopus 로고
    • Scope and utility of hydrogen exchange as a tool for mapping landscapes
    • Jaswal, S. S.; Miranker, A. D. Scope and utility of hydrogen exchange as a tool for mapping landscapes Protein Sci. 2007, 16, 2378-2390
    • (2007) Protein Sci. , vol.16 , pp. 2378-2390
    • Jaswal, S.S.1    Miranker, A.D.2
  • 7
    • 0038271924 scopus 로고    scopus 로고
    • Protein-folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry
    • Konermann, L.; Simmons, D. A. Protein-folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry Mass Spectrom. Rev. 2003, 22, 1-26
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 1-26
    • Konermann, L.1    Simmons, D.A.2
  • 8
    • 49549086897 scopus 로고    scopus 로고
    • Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches
    • Konermann, L.; Tong, X.; Pan, Y. Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches J. Mass Spectrom. 2008, 43, 1021-1036
    • (2008) J. Mass Spectrom. , vol.43 , pp. 1021-1036
    • Konermann, L.1    Tong, X.2    Pan, Y.3
  • 9
    • 84878109818 scopus 로고    scopus 로고
    • Biological insights from hydrogen exchange mass spectrometry
    • Jaswal, S. S. Biological insights from hydrogen exchange mass spectrometry Biochim. Biophys. Acta 2013, 1834, 1188-1201
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1188-1201
    • Jaswal, S.S.1
  • 10
    • 78649674865 scopus 로고    scopus 로고
    • Impact of oxidation on protein therapeutics: Conformational dynamics of intact and oxidized acid-β-glucocerebrosidase at near-physiological pH
    • Bobst, C. E.; Thomas, J. J.; Salinas, P.; Savickas, P.; Kaltashov, I. A. Impact of oxidation on protein therapeutics: Conformational dynamics of intact and oxidized acid-β-glucocerebrosidase at near-physiological pH Protein Sci. 2010, 19, 2366-2378
    • (2010) Protein Sci. , vol.19 , pp. 2366-2378
    • Bobst, C.E.1    Thomas, J.J.2    Salinas, P.3    Savickas, P.4    Kaltashov, I.A.5
  • 11
    • 54749126668 scopus 로고    scopus 로고
    • Detection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches
    • Bobst, C. E.; Abzalimov, R. R.; Houde, D.; Kloczewiak, M.; Mhatre, R.; Berkowitz, S. A.; Kaltashov, I. A. Detection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches Anal. Chem. 2008, 80, 7473-7481
    • (2008) Anal. Chem. , vol.80 , pp. 7473-7481
    • Bobst, C.E.1    Abzalimov, R.R.2    Houde, D.3    Kloczewiak, M.4    Mhatre, R.5    Berkowitz, S.A.6    Kaltashov, I.A.7
  • 12
    • 79954547968 scopus 로고    scopus 로고
    • The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies
    • Houde, D.; Berkowitz, S. A.; Engen, J. R. The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies J. Pharm. Sci. 2011, 100, 2071-2086
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2071-2086
    • Houde, D.1    Berkowitz, S.A.2    Engen, J.R.3
  • 13
    • 76749099328 scopus 로고    scopus 로고
    • Conformation and dynamics of biopharmaceuticals: Transition of mass spectrometry-based tools from academe to industry
    • Kaltashov, I. A.; Bobst, C. E.; Abzalimov, R. R.; Berkowitz, S. A.; Houde, D. Conformation and dynamics of biopharmaceuticals: Transition of mass spectrometry-based tools from academe to industry J. Am. Soc. Mass Spectrom. 2010, 21, 323-337
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 323-337
    • Kaltashov, I.A.1    Bobst, C.E.2    Abzalimov, R.R.3    Berkowitz, S.A.4    Houde, D.5
  • 14
    • 84878108052 scopus 로고    scopus 로고
    • Accessing the reproducibility and specificity of pepsin and other aspartic proteases
    • 10.1016/j.bbapap.2012.10.003
    • Ahn, J.; Cao, M.-J.; Yu, Y. Q.; Engen, J. R. Accessing the reproducibility and specificity of pepsin and other aspartic proteases Biochim. Biophys. Acta 2013, 10.1016/j.bbapap.2012.10.003
    • (2013) Biochim. Biophys. Acta
    • Ahn, J.1    Cao, M.-J.2    Yu, Y.Q.3    Engen, J.R.4
  • 15
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of α -synuclein and other amyloids determined at the amino acid level
    • Del Mar, C.; Greenbaum, E. A.; Mayne, L.; Englander, S. W.; Woods, V. L., Jr. Structure and properties of α -synuclein and other amyloids determined at the amino acid level Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 15477-15482
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, Jr.V.L.5
  • 16
    • 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
  • 17
    • 69849083391 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry with top-down electron capture dissociation for characterizing structural transitions of a 17 kDa protein
    • Pan, J.; Han, J.; Borchers, C. H.; Konermann, L. Hydrogen/deuterium exchange mass spectrometry with top-down electron capture dissociation for characterizing structural transitions of a 17 kDa protein J. Am. Chem. Soc. 2009, 131, 12801-12808
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12801-12808
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 18
    • 67650763014 scopus 로고    scopus 로고
    • Protein conformations can be probed in top-down HDX-MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling
    • Abzalimov, R. R.; Kaplan, D. A.; Easterling, M. L.; Kaltashov, I. A. Protein conformations can be probed in top-down HDX-MS experiments utilizing electron transfer dissociation of protein ions without hydrogen scrambling J. Am. Soc. Mass Spectrom. 2009, 20, 1514-1517
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1514-1517
    • Abzalimov, R.R.1    Kaplan, D.A.2    Easterling, M.L.3    Kaltashov, I.A.4
  • 19
    • 79960003359 scopus 로고    scopus 로고
    • Conformer-specific hydrogen exchange analysis of Aβ(1-42) oligomers by top-down electron capture dissociation mass spectrometry
    • Pan, J.; Han, J.; Borchers, C. H.; Konermann, L. Conformer-specific hydrogen exchange analysis of Aβ(1-42) oligomers by top-down electron capture dissociation mass spectrometry Anal. Chem. 2011, 83, 5386-5393
    • (2011) Anal. Chem. , vol.83 , pp. 5386-5393
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 20
    • 84874978868 scopus 로고    scopus 로고
    • Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation
    • Pan, J.; Borchers, C. H. Top-down structural analysis of posttranslationally modified proteins by Fourier transform ion cyclotron resonance-MS with hydrogen/deuterium exchange and electron capture dissociation Proteomics 2013, 13, 974-981
    • (2013) Proteomics , vol.13 , pp. 974-981
    • Pan, J.1    Borchers, C.H.2
  • 21
    • 0033541119 scopus 로고    scopus 로고
    • Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision-induced dissociation mass spectrometry
    • Deng, Y. Z.; Pan, H.; Smith, D. L. Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision-induced dissociation mass spectrometry J. Am. Chem. Soc. 1999, 121, 1966-1967
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1966-1967
    • Deng, Y.Z.1    Pan, H.2    Smith, D.L.3
  • 22
    • 0035840988 scopus 로고    scopus 로고
    • Site-specific amide hydrogen/deuterium exchange in E. Coli thioredoxins measured by electrospray ionization mass spectrometry
    • Kim, M. Y.; Maier, C. S.; Reed, D. J.; Deinzer, M. L. Site-specific amide hydrogen/deuterium exchange in E. coli thioredoxins measured by electrospray ionization mass spectrometry J. Am. Chem. Soc. 2001, 123, 9860-9866
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9860-9866
    • Kim, M.Y.1    Maier, C.S.2    Reed, D.J.3    Deinzer, M.L.4
  • 23
    • 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
  • 24
    • 80054972554 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein e oligomerization
    • Huang, R. Y. C.; Garai, K.; Frieden, C.; Gross, M. L. Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization Biochemistry 2011, 50, 9273-9282
    • (2011) Biochemistry , vol.50 , pp. 9273-9282
    • Huang, R.Y.C.1    Garai, K.2    Frieden, C.3    Gross, M.L.4
  • 25
    • 84856276827 scopus 로고    scopus 로고
    • Automated hydrogen/deuterium exchange electron transfer dissociation high resolution mass spectrometry measured at single-amide resolution
    • Landgraf, R.; Chalmers, M.; Griffin, P. Automated hydrogen/deuterium exchange electron transfer dissociation high resolution mass spectrometry measured at single-amide resolution J. Am. Soc. Mass Spectrom. 2012, 23, 301-309
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 301-309
    • Landgraf, R.1    Chalmers, M.2    Griffin, P.3
  • 26
    • 2442695484 scopus 로고    scopus 로고
    • Use of statistical methods for estimation of total number of charges in a mass spectrometry experiment
    • Kaur, P.; O'Connor, P. B. Use of statistical methods for estimation of total number of charges in a mass spectrometry experiment Anal. Chem. 2004, 76, 2756-2762
    • (2004) Anal. Chem. , vol.76 , pp. 2756-2762
    • Kaur, P.1    O'Connor, P.B.2
  • 27
    • 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
  • 28
    • 67349186896 scopus 로고    scopus 로고
    • Existence of a noncanonical state of iron-bound transferrin at endosomal pH revealed by hydrogen exchange and mass spectrometry
    • Bobst, C. E.; Zhang, M.; Kaltashov, I. A. Existence of a noncanonical state of iron-bound transferrin at endosomal pH revealed by hydrogen exchange and mass spectrometry J. Mol. Biol. 2009, 388, 954-967
    • (2009) J. Mol. Biol. , vol.388 , pp. 954-967
    • Bobst, C.E.1    Zhang, M.2    Kaltashov, I.A.3
  • 29
    • 84857368753 scopus 로고    scopus 로고
    • Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry
    • Kaltashov, I. A.; Bobst, C. E.; Zhang, M.; Leverence, R.; Gumerov, D. R. Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry Biochim. Biophys. Acta 2012, 1820, 417-426
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 417-426
    • Kaltashov, I.A.1    Bobst, C.E.2    Zhang, M.3    Leverence, R.4    Gumerov, D.R.5
  • 31
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y.; Milne, J. S.; Mayne, L.; Englander, S. W. Primary structure effects on peptide group hydrogen exchange Proteins 1993, 17, 75-86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 32
    • 51349168541 scopus 로고    scopus 로고
    • Electron capture dissociation of electrosprayed protein ions for spatially resolved hydrogen exchange measurements
    • Pan, J.; Han, J.; Borchers, C. H.; Konermann, L. Electron capture dissociation of electrosprayed protein ions for spatially resolved hydrogen exchange measurements J. Am. Chem. Soc. 2008, 130, 11574-11575
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11574-11575
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 33
    • 67749127567 scopus 로고    scopus 로고
    • Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution
    • Zehl, M.; Rand, K. D.; Jensen, O. N.; Jorgensen, T. J. Electron transfer dissociation facilitates the measurement of deuterium incorporation into selectively labeled peptides with single residue resolution J. Am. Chem. Soc. 2008, 130, 17453-17459
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 17453-17459
    • Zehl, M.1    Rand, K.D.2    Jensen, O.N.3    Jorgensen, T.J.4
  • 34
    • 76149130066 scopus 로고    scopus 로고
    • Controlling hydrogen scrambling in multiply charged protein ions during collisional activation: Implications for top-down hydrogen/deuterium exchange MS utilizing collisional activation in the gas phase
    • Abzalimov, R. R.; Kaltashov, I. A. Controlling hydrogen scrambling in multiply charged protein ions during collisional activation: Implications for top-down hydrogen/deuterium exchange MS utilizing collisional activation in the gas phase Anal. Chem. 2010, 82, 942-950
    • (2010) Anal. Chem. , vol.82 , pp. 942-950
    • Abzalimov, R.R.1    Kaltashov, I.A.2
  • 35
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • Cheng, Y.; Zak, O.; Aisen, P.; Harrison, S. C.; Walz, T. Structure of the human transferrin receptor-transferrin complex Cell 2004, 116, 565-576
    • (2004) Cell , vol.116 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 36
    • 80051966207 scopus 로고    scopus 로고
    • How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH
    • Eckenroth, B. E.; Steere, A. N.; Chasteen, N. D.; Everse, S. J.; Mason, A. B. How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 13089-13094
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 13089-13094
    • Eckenroth, B.E.1    Steere, A.N.2    Chasteen, N.D.3    Everse, S.J.4    Mason, A.B.5
  • 37
    • 76649114676 scopus 로고    scopus 로고
    • Protein dynamics and conformational disorder in molecular recognition
    • Mittag, T.; Kay, L. E.; Forman-Kay, J. D. Protein dynamics and conformational disorder in molecular recognition J. Mol. Recognit. 2010, 23, 105-116
    • (2010) J. Mol. Recognit. , vol.23 , pp. 105-116
    • Mittag, T.1    Kay, L.E.2    Forman-Kay, J.D.3
  • 38
    • 79959773723 scopus 로고    scopus 로고
    • Chemodiversity and molecular plasticity: Recognition processes as explored by property spaces
    • Vistoli, G.; Pedretti, A.; Testa, B. Chemodiversity and molecular plasticity: Recognition processes as explored by property spaces Future Med. Chem. 2011, 3, 995-1010
    • (2011) Future Med. Chem. , vol.3 , pp. 995-1010
    • Vistoli, G.1    Pedretti, A.2    Testa, B.3
  • 39
    • 84881027000 scopus 로고    scopus 로고
    • Emerging mass spectrometry-based approaches to probe protein-receptor interactions: Focus on overcoming physiological barriers
    • Kaltashov, I. A.; Bobst, C. E.; Nguyen, S. N.; Wang, S. Emerging mass spectrometry-based approaches to probe protein-receptor interactions: Focus on overcoming physiological barriers Adv. Drug Delivery Rev. 2013, 65, 1020-1030
    • (2013) Adv. Drug Delivery Rev. , vol.65 , pp. 1020-1030
    • Kaltashov, I.A.1    Bobst, C.E.2    Nguyen, S.N.3    Wang, S.4


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