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Volumn 14, Issue 10, 2014, Pages 1249-1258

Top-down mass spectrometry and hydrogen/deuterium exchange for comprehensive structural characterization of interferons: Implications for biosimilars

Author keywords

Biomedicine; Biopharmaceutical; Electron capture dissociation; Hydrogen deuterium exchange; Post translational modification; Top down

Indexed keywords

BIOSIMILAR AGENT; DEUTERIUM; DISULFIDE; HYDROGEN; INTERFERON; PROTEIN VARIANT; RECOMBINANT ALPHA2A INTERFERON; RECOMBINANT ALPHA2B INTERFERON; RECOMBINANT PROTEIN; METHIONINE;

EID: 84899835472     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201300341     Document Type: Article
Times cited : (19)

References (48)
  • 1
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: a summary and pharmacological classification
    • Leader, B., Baca, Q. J., Golan, D. E., Protein therapeutics: a summary and pharmacological classification. Nat. Rev. Drug Discov. 2008, 7, 21-39.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 2
    • 84863218474 scopus 로고    scopus 로고
    • Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars
    • Berkowitz, S. A., Engen, J. R., Mazzeo, J. R., Jones, G. B., Analytical tools for characterizing biopharmaceuticals and the implications for biosimilars. Nat. Rev. Drug Discov. 2012, 11, 527-540.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 527-540
    • Berkowitz, S.A.1    Engen, J.R.2    Mazzeo, J.R.3    Jones, G.B.4
  • 3
    • 34147120188 scopus 로고    scopus 로고
    • Billion dollar babies-biotech drugs as blockbusters
    • Lawrence, S., Billion dollar babies-biotech drugs as blockbusters. Nat. Biotechnol. 2007, 25, 380-382.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 380-382
    • Lawrence, S.1
  • 5
    • 77955412238 scopus 로고    scopus 로고
    • Post-translational modifications differentially affect IgG1 conformation and receptor binding
    • Houde, D., Peng, Y., Berkowitz, S. A., Engen, J. R., Post-translational modifications differentially affect IgG1 conformation and receptor binding. Mol. Cell. Proteomics 2010, 9, 1716-1728.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1716-1728
    • Houde, D.1    Peng, Y.2    Berkowitz, S.A.3    Engen, J.R.4
  • 6
    • 64849114588 scopus 로고    scopus 로고
    • Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry
    • Houde, D., Arndt, J., Domeier, W., Berkowitz, S., Engen, J. R., Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry. Anal. Chem. 2009, 81, 2644-2651.
    • (2009) Anal. Chem. , vol.81 , pp. 2644-2651
    • Houde, D.1    Arndt, J.2    Domeier, W.3    Berkowitz, S.4    Engen, J.R.5
  • 7
    • 34248545257 scopus 로고    scopus 로고
    • Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals
    • Barnes, C. A. S., Lim, A., Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticals. Mass Spectrom. Rev. 2007, 26, 370-388.
    • (2007) Mass Spectrom. Rev. , vol.26 , pp. 370-388
    • Barnes, C.A.S.1    Lim, A.2
  • 8
    • 84861842454 scopus 로고    scopus 로고
    • Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry
    • Beck, A., Sanglier-Cianferani, S., Van Dorsselaer, A., Biosimilar, biobetter, and next generation antibody characterization by mass spectrometry. Anal. Chem. 2012, 84, 4637-4646.
    • (2012) Anal. Chem. , vol.84 , pp. 4637-4646
    • Beck, A.1    Sanglier-Cianferani, S.2    Van Dorsselaer, A.3
  • 9
    • 84871267799 scopus 로고    scopus 로고
    • The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis
    • Thompson, N. J., Rosati, S., Rose, R. J., Heck, A. J. R., The impact of mass spectrometry on the study of intact antibodies: from post-translational modifications to structural analysis. Chem. Commun. 2013, 49, 538-548.
    • (2013) Chem. Commun. , vol.49 , pp. 538-548
    • Thompson, N.J.1    Rosati, S.2    Rose, R.J.3    Heck, A.J.R.4
  • 10
    • 34547751263 scopus 로고    scopus 로고
    • Characterization of variable regions of monoclonal antibodies by top-down mass spectrometry
    • Zhang, Z. Q., Shah, B., Characterization of variable regions of monoclonal antibodies by top-down mass spectrometry. Anal. Chem. 2007, 79, 5723-5729.
    • (2007) Anal. Chem. , vol.79 , pp. 5723-5729
    • Zhang, Z.Q.1    Shah, B.2
  • 11
    • 82555170557 scopus 로고    scopus 로고
    • Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry
    • Tsybin, Y. O., Fornelli, L., Stoermer, C., Luebeck, M. et al., Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry. Anal. Chem. 2011, 83, 8919-8927.
    • (2011) Anal. Chem. , vol.83 , pp. 8919-8927
    • Tsybin, Y.O.1    Fornelli, L.2    Stoermer, C.3    Luebeck, M.4
  • 12
    • 84870653816 scopus 로고    scopus 로고
    • Analysis of intact monoclonal antibody IgG1 by electron transfer dissociation orbitrap FTMS
    • Fornelli, L., Damoc, E., Thomas, P. M., Kelleher, N. L. et al., Analysis of intact monoclonal antibody IgG1 by electron transfer dissociation orbitrap FTMS. Mol. Cell. Proteomics 2012, 11, 1758-1767.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1758-1767
    • Fornelli, L.1    Damoc, E.2    Thomas, P.M.3    Kelleher, N.L.4
  • 13
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann, L., Pan, J., Liu, Y., 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.3
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamics by mass spectrometry
    • Kaltashov, I. A., Eyles, S. J., Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom. Rev. 2002, 21, 37-71.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 17
    • 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
  • 18
    • 0242386421 scopus 로고    scopus 로고
    • Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins
    • Cravello, L., Lascoux, D., Forest, E., Use of different proteases working in acidic conditions to improve sequence coverage and resolution in hydrogen/deuterium exchange of large proteins. Rapid Commun. Mass Spectrom. 2003, 17, 2387-2393.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2387-2393
    • Cravello, L.1    Lascoux, D.2    Forest, E.3
  • 19
    • 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., Structure and properties of α-synuclein and other amyloids determined at the amino acid level. Proc. Natl. Acad. Sci. USA 2005, 102, 15477-15482.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 20
    • 0031018084 scopus 로고    scopus 로고
    • Probing the noncovalent structure of proteins by amide hydrogen exchange mass spectrometry
    • Smith, D. L., Deng, Y., Zhang, Z., Probing the noncovalent structure of proteins by amide hydrogen exchange mass spectrometry. J. Mass Spectrom. 1997, 32, 135-146.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 21
    • 76149083241 scopus 로고    scopus 로고
    • Dynamics of the β2-adrenergic G-protein coupled receptor revealed by hydrogen-deuterium exchange
    • Zhang, X., Chien, E. Y. T., Chalmers, M. J., Pascal, B. D. et al., Dynamics of the β2-adrenergic G-protein coupled receptor revealed by hydrogen-deuterium exchange. Anal. Chem. 2010, 82, 1100-1108.
    • (2010) Anal. Chem. , vol.82 , pp. 1100-1108
    • Zhang, X.1    Chien, E.Y.T.2    Chalmers, M.J.3    Pascal, B.D.4
  • 22
    • 84874701192 scopus 로고    scopus 로고
    • Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry
    • Rand, K. D., Pinpointing changes in higher-order protein structure by hydrogen/deuterium exchange coupled to electron transfer dissociation mass spectrometry. Int. J. Mass Spectrom. 2013, 338, 2-10.
    • (2013) Int. J. Mass Spectrom. , vol.338 , pp. 2-10
    • Rand, K.D.1
  • 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., Jørgensen, 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    Jørgensen, T.J.D.4
  • 24
    • 84856276827 scopus 로고    scopus 로고
    • Automated hydrogen/deuterium exchange electron transfer dissociation high resolution mass spectrometry measured at single-amide resolution
    • Landgraf, R. R., Chalmers, M. J., Griffin, P. R., 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.R.1    Chalmers, M.J.2    Griffin, P.R.3
  • 25
    • 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
  • 26
    • 84860430705 scopus 로고    scopus 로고
    • Structure and dynamics of small soluble A beta(1-40) oligomers studied by top-down hydrogen exchange mass spectrometry
    • Pan, J., Han, J., Borchers, C. H., Konermann, L., Structure and dynamics of small soluble A beta(1-40) oligomers studied by top-down hydrogen exchange mass spectrometry. Biochemistry 2012, 51, 3694-3703.
    • (2012) Biochemistry , vol.51 , pp. 3694-3703
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 27
    • 84865493244 scopus 로고    scopus 로고
    • Top-down hydrogen/deuterium exchange and ECD-stitched FTICR-MS for probing structural dynamics of a 29-kDa enzyme
    • Pan, J. X., Han, J., Borchers, C. H., Top-down hydrogen/deuterium exchange and ECD-stitched FTICR-MS for probing structural dynamics of a 29-kDa enzyme. Int. J. Mass Spectrom. 2012, 325, 130-138.
    • (2012) Int. J. Mass Spectrom. , vol.325 , pp. 130-138
    • Pan, J.X.1    Han, J.2    Borchers, C.H.3
  • 28
    • 84861181306 scopus 로고    scopus 로고
    • Spatially resolved protein hydrogen exchange measured by subzero-cooled chip-based nanoelectrospray ionization tandem mass spectrometry
    • Amon, S., Trelle, M. B., Jensen, O. N., Jorgensen, T. J. D., Spatially resolved protein hydrogen exchange measured by subzero-cooled chip-based nanoelectrospray ionization tandem mass spectrometry. Anal. Chem. 2012, 84, 4467-4473.
    • (2012) Anal. Chem. , vol.84 , pp. 4467-4473
    • Amon, S.1    Trelle, M.B.2    Jensen, O.N.3    Jorgensen, T.J.D.4
  • 30
    • 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. Proc. Natl. Acad. Sci. USA 2004, 101, 9528-9533.
    • (2004) Proc. Natl. Acad. Sci. USA , 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
  • 31
    • 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., Jørgensen, 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    Jørgensen, T.J.D.4
  • 32
    • 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., Jørgensen, T. J. D., 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    Jørgensen, T.J.D.4
  • 33
    • 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
  • 34
    • 78049502162 scopus 로고    scopus 로고
    • Real-time hydrogen/deuterium exchange kinetics via supercharged electrospray ionization tandem mass spectrometry
    • Sterling, H. J., Williams, E. R., Real-time hydrogen/deuterium exchange kinetics via supercharged electrospray ionization tandem mass spectrometry. Anal. Chem. 2010, 82, 9050-9057.
    • (2010) Anal. Chem. , vol.82 , pp. 9050-9057
    • Sterling, H.J.1    Williams, E.R.2
  • 35
    • 84861181306 scopus 로고    scopus 로고
    • Spatially resolved protein hydrogen exchange measured by subzero-cooled chip-based nanoelectrospray ionization tandem mass spectrometry
    • Amon, S., Trelle, M. B., Jensen, O. N., Jørgensen, T. J. D., Spatially resolved protein hydrogen exchange measured by subzero-cooled chip-based nanoelectrospray ionization tandem mass spectrometry. Anal. Chem. 2012, 84, 4467-4473.
    • (2012) Anal. Chem. , vol.84 , pp. 4467-4473
    • Amon, S.1    Trelle, M.B.2    Jensen, O.N.3    Jørgensen, T.J.D.4
  • 36
    • 14744272834 scopus 로고    scopus 로고
    • Intramolecular migration of amide hydrogens in protonated peptides upon collisional activation
    • Jørgensen, T. J. D., Gårdsvoll, 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
    • Jørgensen, T.J.D.1    Gårdsvoll, H.2    Ploug, M.3    Roepstorff, P.4
  • 37
    • 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
  • 38
    • 77958068942 scopus 로고    scopus 로고
    • Characterizing short-lived protein folding intermediates by top-down hydrogen exchange mass spectrometry
    • Pan, J., Han, J., Borchers, C. H., Konermann, L., Characterizing short-lived protein folding intermediates by top-down hydrogen exchange mass spectrometry. Anal. Chem. 2010, 82, 8591-8597.
    • (2010) Anal. Chem. , vol.82 , pp. 8591-8597
    • Pan, J.1    Han, J.2    Borchers, C.H.3    Konermann, L.4
  • 39
    • 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. X., 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.X.1    Borchers, C.H.2
  • 40
    • 33747333617 scopus 로고    scopus 로고
    • Allosteric activation of coagulation factor VIIa visualized by hydrogen exchange
    • Rand, K. D., Jorgensen, T. J. D., Olsen, O. H., Persson, E. et al., Allosteric activation of coagulation factor VIIa visualized by hydrogen exchange. J. Biol. Chem. 2006, 281, 23018-23024.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23018-23024
    • Rand, K.D.1    Jorgensen, T.J.D.2    Olsen, O.H.3    Persson, E.4
  • 41
    • 33947720248 scopus 로고    scopus 로고
    • A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation
    • Olsen, O. H., Rand, K. D., Ostergaard, H., Persson, E., A combined structural dynamics approach identifies a putative switch in factor VIIa employed by tissue factor to initiate blood coagulation. Protein Sci. 2007, 16, 671-682.
    • (2007) Protein Sci. , vol.16 , pp. 671-682
    • Olsen, O.H.1    Rand, K.D.2    Ostergaard, H.3    Persson, E.4
  • 42
    • 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. et al., 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
  • 43
    • 77950236865 scopus 로고    scopus 로고
    • Conformational changes in oxidatively stressed monoclonal antibodies studied by hydrogen exchange mass spectrometry
    • Burkitt, W., Domann, P., O'Connor, G., Conformational changes in oxidatively stressed monoclonal antibodies studied by hydrogen exchange mass spectrometry. Protein Sci. 2010, 19, 826-835.
    • (2010) Protein Sci. , vol.19 , pp. 826-835
    • Burkitt, W.1    Domann, P.2    O'Connor, G.3
  • 44
    • 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
  • 45
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-express
    • Weis, D. D., Engen, J. R., Kass, I. J., Semi-automated data processing of hydrogen exchange mass spectra using HX-express. J. Am. Soc. Mass Spectrom. 2006, 17, 1700-1703.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 46
    • 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
  • 47
    • 0031566032 scopus 로고    scopus 로고
    • The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution
    • Klaus, W., Gsell, B., Labhardt, A. M., Wipf, B., Senn, H., The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution. J. Mol. Biol. 1997, 274, 661-675.
    • (1997) J. Mol. Biol. , vol.274 , pp. 661-675
    • Klaus, W.1    Gsell, B.2    Labhardt, A.M.3    Wipf, B.4    Senn, H.5
  • 48
    • 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. Comp. Chem. 1998, 19, 319-333.
    • (1998) J. Comp. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2


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