메뉴 건너뛰기




Volumn 366, Issue 1, 2007, Pages 18-28

Characterizing protein structure in amorphous solids using hydrogen/deuterium exchange with mass spectrometry

Author keywords

Amorphous solids; FTIR; Hydrogen deuterium exchange; Mass spectrometry; Protein lyophilization; Protein structure

Indexed keywords

AMORPHOUS MATERIALS; CALCIUM CHLORIDE; ELECTROSPRAY IONIZATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HUMIDITY CONTROL; INFRARED DEVICES; MASS SPECTROMETRY; NEAR INFRARED SPECTROSCOPY;

EID: 34248566786     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.03.041     Document Type: Article
Times cited : (38)

References (33)
  • 1
    • 33645170297 scopus 로고    scopus 로고
    • Excipients for use in lyophilized pharmaceutical peptide, protein, and other bioproducts
    • Costantino H.R. Excipients for use in lyophilized pharmaceutical peptide, protein, and other bioproducts. Biotechnol. Pharmaceut. Aspects 2 (2004) 139-228
    • (2004) Biotechnol. Pharmaceut. Aspects , vol.2 , pp. 139-228
    • Costantino, H.R.1
  • 4
    • 33745926621 scopus 로고    scopus 로고
    • Freezing- and drying-induced perturbations of protein structure and mechanisms of protein protection by stabilizing additives
    • Carpenter J.F., Izutsu K.-I., and Randolph T.W. Freezing- and drying-induced perturbations of protein structure and mechanisms of protein protection by stabilizing additives. Drugs Pharmaceut. Sci. 137 (2004) 147-186
    • (2004) Drugs Pharmaceut. Sci. , vol.137 , pp. 147-186
    • Carpenter, J.F.1    Izutsu, K.-I.2    Randolph, T.W.3
  • 5
    • 0032078387 scopus 로고    scopus 로고
    • Application of infrared spectroscopy to development of stable lyophilized protein formulations
    • Carpenter J.F., Prestrelski S.J., and Dong A. Application of infrared spectroscopy to development of stable lyophilized protein formulations. Eur. J. Pharmaceut. Biopharmaceut. 45 (1998) 231-238
    • (1998) Eur. J. Pharmaceut. Biopharmaceut. , vol.45 , pp. 231-238
    • Carpenter, J.F.1    Prestrelski, S.J.2    Dong, A.3
  • 6
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong A., Prestrelski S.J., Allison S.D., and Carpenter J.F. Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J. Pharmaceut. Sci. 84 (1995) 415-424
    • (1995) J. Pharmaceut. Sci. , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 7
    • 1842482434 scopus 로고    scopus 로고
    • Raman spectroscopic characterization of drying-induced structural changes in a therapeutic antibody: correlating structural changes with long-term stability
    • Sane S.U., Wong R., and Hsu C.C. Raman spectroscopic characterization of drying-induced structural changes in a therapeutic antibody: correlating structural changes with long-term stability. J. Pharmaceut. Sci. 93 (2004) 1005-1018
    • (2004) J. Pharmaceut. Sci. , vol.93 , pp. 1005-1018
    • Sane, S.U.1    Wong, R.2    Hsu, C.C.3
  • 8
    • 33645980951 scopus 로고    scopus 로고
    • Near-infrared analysis of protein secondary structure in aqueous solutions and freeze-dried solids
    • Izutsu K.-I., Fujimaki Y., Kuwabara A., Hiyama Y., Yomota C., and Aoyagi N. Near-infrared analysis of protein secondary structure in aqueous solutions and freeze-dried solids. J. Pharmaceut. Sci. 95 (2006) 781-789
    • (2006) J. Pharmaceut. Sci. , vol.95 , pp. 781-789
    • Izutsu, K.-I.1    Fujimaki, Y.2    Kuwabara, A.3    Hiyama, Y.4    Yomota, C.5    Aoyagi, N.6
  • 9
    • 27644477359 scopus 로고    scopus 로고
    • Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy
    • Bai S., Nayar R., Carpenter J.F., and Manning M.C. Noninvasive determination of protein conformation in the solid state using near infrared (NIR) spectroscopy. J. Pharmaceut. Sci. 94 (2005) 2030-2038
    • (2005) J. Pharmaceut. Sci. , vol.94 , pp. 2030-2038
    • Bai, S.1    Nayar, R.2    Carpenter, J.F.3    Manning, M.C.4
  • 10
    • 33645505791 scopus 로고    scopus 로고
    • Solid-state NMR studies of the structure, dynamics, and assembly of b-sheet membrane peptides and a-helical membrane proteins with antibiotic activities
    • Hong M. Solid-state NMR studies of the structure, dynamics, and assembly of b-sheet membrane peptides and a-helical membrane proteins with antibiotic activities. Accounts Chem. Res. 39 (2006) 176-183
    • (2006) Accounts Chem. Res. , vol.39 , pp. 176-183
    • Hong, M.1
  • 11
    • 4744357287 scopus 로고    scopus 로고
    • Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward
    • McDermott A.E. Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward. Curr. Opin. Struct. Biol. 14 (2004) 554-561
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 554-561
    • McDermott, A.E.1
  • 12
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella S.J., and Marassi F.M. Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 104 (2004) 3587-3606
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 13
    • 0346511459 scopus 로고    scopus 로고
    • Recent advances in high-resolution solid-state NMR spectroscopy
    • Schwalbe H., and Bielecki A. Recent advances in high-resolution solid-state NMR spectroscopy. Angew. Chem. International Edition 40 (2001) 2045-2050
    • (2001) Angew. Chem. International Edition , vol.40 , pp. 2045-2050
    • Schwalbe, H.1    Bielecki, A.2
  • 14
    • 0036816798 scopus 로고    scopus 로고
    • Solid-state NMR studies of the structure and mechanisms of proteins
    • Thompson L.K. Solid-state NMR studies of the structure and mechanisms of proteins. Curr. Opin. Struct. Biol. 12 (2002) 661-669
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 661-669
    • Thompson, L.K.1
  • 15
    • 0033655078 scopus 로고    scopus 로고
    • Investigating the higher order structure of proteins: hydrogen exchange, proteolytic fragmentation, and mass spectrometry
    • Engen J.R., and Smith D.L. Investigating the higher order structure of proteins: hydrogen exchange, proteolytic fragmentation, and mass spectrometry. Methods Mol. Biol. (Totowa, New Jersey) 146 (2000) 95-112
    • (2000) Methods Mol. Biol. (Totowa, New Jersey) , vol.146 , pp. 95-112
    • Engen, J.R.1    Smith, D.L.2
  • 17
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales T.E., and Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrometry Rev. 25 (2006) 158-170
    • (2006) Mass Spectrometry Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 18
    • 0028029812 scopus 로고
    • Protein structure in the lyophilized state: A hydrogen isotope exchange/NMR study with bovine pancreatic trypsin inhibitor
    • Desai U.R., Osterhout J.J., and Klibanov A.M. Protein structure in the lyophilized state: A hydrogen isotope exchange/NMR study with bovine pancreatic trypsin inhibitor. J. Am. Chem. Soc. 116 (1994) 9420-9422
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9420-9422
    • Desai, U.R.1    Osterhout, J.J.2    Klibanov, A.M.3
  • 19
    • 1542724789 scopus 로고    scopus 로고
    • Fourier transformed infrared spectroscopic investigation of protein conformation in spray-dried protein/trehalose powders
    • French D.L., Arakawa T., and Li T. Fourier transformed infrared spectroscopic investigation of protein conformation in spray-dried protein/trehalose powders. Biopolymers 73 (2004) 524-531
    • (2004) Biopolymers , vol.73 , pp. 524-531
    • French, D.L.1    Arakawa, T.2    Li, T.3
  • 21
    • 33749984171 scopus 로고    scopus 로고
    • Increasing application of X-ray powder diffraction in the pharmaceutical industry
    • Litteer B., and Beckers D. Increasing application of X-ray powder diffraction in the pharmaceutical industry. American Laboratory (Shelton, CT, United States) 37 (2005) 22-24
    • (2005) American Laboratory (Shelton, CT, United States) , vol.37 , pp. 22-24
    • Litteer, B.1    Beckers, D.2
  • 22
    • 0036253941 scopus 로고    scopus 로고
    • X-ray powder diffraction of pharmaceutical materials
    • 78, 80
    • Brittain H.G. X-ray powder diffraction of pharmaceutical materials. American Pharmaceutical Review 5 (2002) 74-76 78, 80
    • (2002) American Pharmaceutical Review , vol.5 , pp. 74-76
    • Brittain, H.G.1
  • 23
    • 0024583565 scopus 로고
    • Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: effects of calcium and magnesium binding
    • Trewhella J., Liddle W.K., Heidorn D.B., and Strynadka N. Calmodulin and troponin C structures studied by Fourier transform infrared spectroscopy: effects of calcium and magnesium binding. Biochemistry 28 (1989) 1294-1301
    • (1989) Biochemistry , vol.28 , pp. 1294-1301
    • Trewhella, J.1    Liddle, W.K.2    Heidorn, D.B.3    Strynadka, N.4
  • 24
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the Area of Overlap between Second-Derivative Amide I Infrared Spectra To Determine the Structural Similarity of a Protein in Different States
    • Kendrick B.S., Dong A., Allison S.D., Manning M.C., and Carpenter J.F. Quantitation of the Area of Overlap between Second-Derivative Amide I Infrared Spectra To Determine the Structural Similarity of a Protein in Different States. J. Pharmaceut. Sci. 85 (1996) 155-158
    • (1996) J. Pharmaceut. Sci. , vol.85 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.2    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 25
    • 0003127079 scopus 로고
    • Saturated salt solutions for maintaining specified relative humidities
    • Nyqvist H. Saturated salt solutions for maintaining specified relative humidities. Int. J. Pharmaceut. Technol. Product Manufacture 4 (1983) 47-48
    • (1983) Int. J. Pharmaceut. Technol. Product Manufacture , vol.4 , pp. 47-48
    • Nyqvist, H.1
  • 26
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang Z., and Smith D.L. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2 (1993) 522-531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 27
    • 0026046615 scopus 로고
    • Fourier transform infrared spectroscopic studies of calcium-binding proteins
    • Jackson M., Haris P.I., and Chapman D. Fourier transform infrared spectroscopic studies of calcium-binding proteins. Biochemistry 30 (1991) 9681-9686
    • (1991) Biochemistry , vol.30 , pp. 9681-9686
    • Jackson, M.1    Haris, P.I.2    Chapman, D.3
  • 28
    • 0001510590 scopus 로고
    • Ion formation from charged droplets: roles of geometry, energy, and time
    • Fenn J.B. Ion formation from charged droplets: roles of geometry, energy, and time. J. Am. Soc. Mass Spectrometry 4 (1993) 524-535
    • (1993) J. Am. Soc. Mass Spectrometry , vol.4 , pp. 524-535
    • Fenn, J.B.1
  • 29
    • 9744270012 scopus 로고    scopus 로고
    • Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry
    • Busenlehner L.S., and Armstrong R.N. Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry. Arch. Biochem. Biophys. 433 (2005) 34-46
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 34-46
    • Busenlehner, L.S.1    Armstrong, R.N.2
  • 30
    • 0346431875 scopus 로고    scopus 로고
    • Probing Ca2+-induced conformational changes in porcine calmodulin by H/D exchange and ESI-MS: Effect of cations and ionic strength
    • Zhu M.M., Rempel D.L., Zhao J., Giblin D.E., and Gross M.L. Probing Ca2+-induced conformational changes in porcine calmodulin by H/D exchange and ESI-MS: Effect of cations and ionic strength. Biochemistry 42 (2003) 15388-15397
    • (2003) Biochemistry , vol.42 , pp. 15388-15397
    • Zhu, M.M.1    Rempel, D.L.2    Zhao, J.3    Giblin, D.E.4    Gross, M.L.5
  • 31
    • 0033473742 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry and hydrogen/deuterium exchange for probing the interaction of calmodulin with calcium
    • Nemirovskiy O., Giblin D.E., and Gross M.L. Electrospray ionization mass spectrometry and hydrogen/deuterium exchange for probing the interaction of calmodulin with calcium. J. Am. Soc. Mass Spectrometry 10 (1999) 711-718
    • (1999) J. Am. Soc. Mass Spectrometry , vol.10 , pp. 711-718
    • Nemirovskiy, O.1    Giblin, D.E.2    Gross, M.L.3
  • 32
    • 1542289847 scopus 로고    scopus 로고
    • Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of Staphylococcus aureus aldolase
    • Pan H., and Smith D.L. Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of Staphylococcus aureus aldolase. Methods Enzymol. 380 (2004) 285-308
    • (2004) Methods Enzymol. , vol.380 , pp. 285-308
    • Pan, H.1    Smith, D.L.2
  • 33
    • 0037333292 scopus 로고    scopus 로고
    • Downsizing improves sensitivity 100-fold for hydrogen exchange-mass spectrometry
    • Wang L., and Smith D.L. Downsizing improves sensitivity 100-fold for hydrogen exchange-mass spectrometry. Anal. Biochem. 314 (2003) 46-53
    • (2003) Anal. Biochem. , vol.314 , pp. 46-53
    • Wang, L.1    Smith, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.