메뉴 건너뛰기




Volumn , Issue , 2011, Pages 263-292

Spectroscopy of Vaccines

Author keywords

Circular dichroism (CD), frequent method change estimation, structure of proteins and DNA; Immunogen characterization, vaccine spectroscopy energy interaction, electromagnetic radiation, or sound with matter; Vaccine "dynamics" emerging technique, dynamic behavior of macromolecules, ultrasonic spectroscopy

Indexed keywords


EID: 84886166724     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118023648.ch10     Document Type: Chapter
Times cited : (2)

References (75)
  • 1
    • 53549111888 scopus 로고    scopus 로고
    • Physical characterization of clostridium difficile toxins and toxoids: Effect of the formaldehyde crosslinking on thermal stability
    • Salnikova MS, Joshi SB, Rytting JH,Warny M, and Middaugh CR. Physical characterization of clostridium difficile toxins and toxoids: Effect of the formaldehyde crosslinking on thermal stability. J. Pharm. Sci. 2008;97:3735-3752.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 3735-3752
    • Salnikova, M.S.1    Joshi, S.B.2    Rytting, J.H.3    Warny, M.4    Middaugh, C.R.5
  • 2
    • 33745359812 scopus 로고    scopus 로고
    • A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine
    • Peek LJ. Brandau DT, Jones LS, Joshi SB, and Middaugh CR. A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine. Vaccine 2006;24:5839-5851.
    • (2006) Vaccine , vol.24 , pp. 5839-5851
    • Peek, L.J.1    Brandau, D.T.2    Jones, L.S.3    Joshi, S.B.4    Middaugh, C.R.5
  • 3
    • 33846131223 scopus 로고    scopus 로고
    • A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine
    • Peek LJ. Brey RN, and Middaugh CR. A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine. J. Pharm. Sci. 2007;96:44-60.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 44-60
    • Peek, L.J.1    Brey, R.N.2    Middaugh, C.R.3
  • 5
    • 0036285313 scopus 로고    scopus 로고
    • Pharmaceutical and immunological evaluation of a single-shot hepatitis B vaccine formulated with PLGA microspheres
    • Shi L, Caulfield MJ, Chern RT, Wilson RA, Sanyal G, and Volkin DB. Pharmaceutical and immunological evaluation of a single-shot hepatitis B vaccine formulated with PLGA microspheres. J. Pharm. Sci. 2002;91:1019-1035.
    • (2002) J. Pharm. Sci. , vol.91 , pp. 1019-1035
    • Shi, L.1    Caulfield, M.J.2    Chern, R.T.3    Wilson, R.A.4    Sanyal, G.5    Volkin, D.B.6
  • 7
    • 33745820802 scopus 로고    scopus 로고
    • Conformational stability and disassembly of Norwalk virus like particles: Effect of pH and temperature
    • Ausar SF, Foubert TR, Hudson MH, Vedvick TS, and Middaugh CR. Conformational stability and disassembly of Norwalk virus like particles: Effect of pH and temperature. J. Biol. Chem. 2006;281:19478-19488.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19478-19488
    • Ausar, S.F.1    Foubert, T.R.2    Hudson, M.H.3    Vedvick, T.S.4    Middaugh, C.R.5
  • 11
    • 34248214194 scopus 로고    scopus 로고
    • High-throughput screening of stabilizers for respiratory syncytial virus: Identification of stabilizers and their effects on the conformational thermostability of viral particles
    • Ausar SF, Espina M, Brock J, Thyagarayapuran N, Repetto R, Khandke L, and Middaugh CR, High-throughput screening of stabilizers for respiratory syncytial virus: Identification of stabilizers and their effects on the conformational thermostability of viral particles. Hum. Vaccines 2007;3:94-103.
    • (2007) Hum. Vaccines , vol.3 , pp. 94-103
    • Ausar, S.F.1    Espina, M.2    Brock, J.3    Thyagarayapuran, N.4    Repetto, R.5    Khandke, L.6    Middaugh, C.R.7
  • 14
    • 0031011382 scopus 로고    scopus 로고
    • Size and conformational stability of the hepatitis A virus used to prepare VAQTA, a highly purified inactivated vaccine
    • Volkin DB, Burke CJ, Marfia KE, Oswald CB, Wolanski B, and Middaugh CR. Size and conformational stability of the hepatitis A virus used to prepare VAQTA, a highly purified inactivated vaccine. J. Pharm. Sci. 1997;86:666-673.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 666-673
    • Volkin, D.B.1    Burke, C.J.2    Marfia, K.E.3    Oswald, C.B.4    Wolanski, B.5    Middaugh, C.R.6
  • 16
    • 35348943833 scopus 로고    scopus 로고
    • Analysis of cationic-lipid-plasmid-DNA complexes
    • Middaugh CR and Ramsey JD. Analysis of cationic-lipid-plasmid-DNA complexes. Anal. Chem. 2007;79:7240-7248.
    • (2007) Anal. Chem. , vol.79 , pp. 7240-7248
    • Middaugh, C.R.1    Ramsey, J.D.2
  • 17
    • 84934437177 scopus 로고    scopus 로고
    • Spectroscopic methods for the physical characterization and formulation of nonviral gene delivery systems
    • Ausar SF, Joshi SB, and Middaugh CR. Spectroscopic methods for the physical characterization and formulation of nonviral gene delivery systems. Methods Mol. Biol. 2008;434:55-80.
    • (2008) Methods Mol. Biol. , vol.434 , pp. 55-80
    • Ausar, S.F.1    Joshi, S.B.2    Middaugh, C.R.3
  • 19
    • 0028062558 scopus 로고
    • Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy
    • Haris PI and Chapman D. Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy. Methods Mol. Biol. 1994;22:183-202.
    • (1994) Methods Mol. Biol. , vol.22 , pp. 183-202
    • Haris, P.I.1    Chapman, D.2
  • 21
    • 17144427675 scopus 로고    scopus 로고
    • Effects of adsorption to aluminum salt adjuvants on the structure and stability of model protein antigens
    • Jones LS, Peek LJ, Power J, Markham A, Yazzie B, and Middaugh CR. Effects of adsorption to aluminum salt adjuvants on the structure and stability of model protein antigens. J. Biol. Chem. 2005;280:13406-13414.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13406-13414
    • Jones, L.S.1    Peek, L.J.2    Power, J.3    Markham, A.4    Yazzie, B.5    Middaugh, C.R.6
  • 24
    • 33847690155 scopus 로고    scopus 로고
    • Secondary structure analysis of HIV-1-gp41 in solution and adsorbed to aluminum hydroxide by Fourier transform infrared spectroscopy
    • Agopian A, Ronzon F, Sauzeat E, Sodoyer R, El Habib R, Buchet R, and Chevalier M. Secondary structure analysis of HIV-1-gp41 in solution and adsorbed to aluminum hydroxide by Fourier transform infrared spectroscopy. Biochim. Biophys. Acta 2007;1774:351-358.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 351-358
    • Agopian, A.1    Ronzon, F.2    Sauzeat, E.3    Sodoyer, R.4    El Habib, R.5    Buchet, R.6    Chevalier, M.7
  • 25
    • 0032743863 scopus 로고    scopus 로고
    • Direct Biophys.ical characterization of human apolipoprotein A-1 in ISCOMs
    • Chen H, and Sanyal G. Direct Biophys.ical characterization of human apolipoprotein A-1 in ISCOMs. J. Pharm. Sci. 1999;88:1122-1126.
    • (1999) J. Pharm. Sci. , vol.88 , pp. 1122-1126
    • Chen, H.1    Sanyal, G.2
  • 26
    • 33645294911 scopus 로고    scopus 로고
    • Secondary structures of proteins adsorbed onto aluminum hydroxide: Infrared spectroscopic analysis of proteins from low solution concentrations
    • Dong A, Jones LS, Kerwin BA, Krishnan S, and Carpenter JF. Secondary structures of proteins adsorbed onto aluminum hydroxide: Infrared spectroscopic analysis of proteins from low solution concentrations. Anal. Biochem. 2006;351:282-289.
    • (2006) Anal. Biochem. , vol.351 , pp. 282-289
    • Dong, A.1    Jones, L.S.2    Kerwin, B.A.3    Krishnan, S.4    Carpenter, J.F.5
  • 27
    • 33947538420 scopus 로고    scopus 로고
    • Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants
    • Peek, LJ, Martin T, Elk NC, Pegram S, and Middaugh CR. Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants. J. Pharm. Sci. 2007;96:547-557.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 547-557
    • Peek, L.J.1    Martin, T.2    Elk, N.C.3    Pegram, S.4    Middaugh, C.R.5
  • 28
    • 63749131101 scopus 로고    scopus 로고
    • Correlation of ATR-FTIR spectra and particle sizes of temperature-induced protein aggregates
    • Meyer BK, Lu W, Mach H, and Shi L. Correlation of ATR-FTIR spectra and particle sizes of temperature-induced protein aggregates. Amer. Lab. 2008;40(1):12-15.
    • (2008) Amer. Lab. , vol.40 , Issue.1 , pp. 12-15
    • Meyer, B.K.1    Lu, W.2    Mach, H.3    Shi, L.4
  • 29
    • 37649018757 scopus 로고    scopus 로고
    • Structural characterisation of the hepatitis C envelope glycoprotein E1 ectodomain derived from a mammalian and a yeast expression system
    • Lorent E, Bierau H, Engelborghs Y, Verheyden G, and Bosman F. Structural characterisation of the hepatitis C envelope glycoprotein E1 ectodomain derived from a mammalian and a yeast expression system. Vaccine 2008;26:399-410.
    • (2008) Vaccine , vol.26 , pp. 399-410
    • Lorent, E.1    Bierau, H.2    Engelborghs, Y.3    Verheyden, G.4    Bosman, F.5
  • 30
    • 33845641277 scopus 로고    scopus 로고
    • Spectroscopic study of conformational changes accompanying self-assembly of HCV core protein
    • Rodriguez-Casado A, Molina M, and Carmona P. Spectroscopic study of conformational changes accompanying self-assembly of HCV core protein. Proteins 2007;66:110-117.
    • (2007) Proteins , vol.66 , pp. 110-117
    • Rodriguez-Casado, A.1    Molina, M.2    Carmona, P.3
  • 31
    • 34147110914 scopus 로고    scopus 로고
    • Formulation and evaluation of an oral melanoma vaccine
    • Lai YH and D'Souza MJ. Formulation and evaluation of an oral melanoma vaccine. J. Microencapsul. 2007;24:235-252.
    • (2007) J. Microencapsul. , vol.24 , pp. 235-252
    • Lai, Y.H.1    D'Souza, M.J.2
  • 36
    • 0036174061 scopus 로고    scopus 로고
    • Differential scanning calorimetric studies of the thermal stability of plasmid DNA complexed with cationic lipids and polymers
    • Lobo B, Rogers S, Choosakoonkriang S, Smith JG, Koe G, and Middaugh CR. Differential scanning calorimetric studies of the thermal stability of plasmid DNA complexed with cationic lipids and polymers. J. Pharm. Sci. 2001;91:454-466.
    • (2001) J. Pharm. Sci. , vol.91 , pp. 454-466
    • Lobo, B.1    Rogers, S.2    Choosakoonkriang, S.3    Smith, J.G.4    Koe, G.5    Middaugh, C.R.6
  • 37
    • 0037417751 scopus 로고    scopus 로고
    • Protein and DNA residue orientations in the filamentous virus Pf1 determined by polarized Raman and polarized FTIR spectroscopy
    • Tsuboi M, Kubo Y, Ikeda T, Overman SA, Osman O, and Thomas GJ, Jr. Protein and DNA residue orientations in the filamentous virus Pf1 determined by polarized Raman and polarized FTIR spectroscopy. BioChemistry 2003;42:940-950.
    • (2003) BioChemistry , vol.42 , pp. 940-950
    • Tsuboi, M.1    Kubo, Y.2    Ikeda, T.3    Overman, S.A.4    Osman, O.5    Thomas, G.J.Jr.6
  • 38
  • 39
    • 0032986173 scopus 로고    scopus 로고
    • Raman spectroscopy of protein and nucleic acid assemblies
    • Thomas GJ, Jr. Raman spectroscopy of protein and nucleic acid assemblies. Annu. Rev. Biophys. Biomol. Struct. 1999;28:1-27.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 1-27
    • Thomas, G.J.Jr.1
  • 40
    • 36849073223 scopus 로고    scopus 로고
    • Raman spectroscopy of protein Pharmaceuticals
    • Wen ZQ. Raman spectroscopy of protein Pharmaceuticals. J. Pharm. Sci. 2007;96:2861-2878.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 2861-2878
    • Wen, Z.Q.1
  • 42
    • 0036060783 scopus 로고    scopus 로고
    • Adsorption of polyethyleneimine on silver nanoparticles and its interaction with a plasmid DNA: A surface-enhanced Raman scattering study
    • Sanchez-Cortes S. Berenguel RM, Madejon, A, and Perez-Mendez M. Adsorption of polyethyleneimine on silver nanoparticles and its interaction with a plasmid DNA: A surface-enhanced Raman scattering study. Biomacromolecules 2002;3:655-660.
    • (2002) Biomacromolecules , vol.3 , pp. 655-660
    • Sanchez-Cortes, S.1    Berenguel, R.M.2    Madejon, A.3    Perez-Mendez, M.4
  • 43
    • 33846149684 scopus 로고    scopus 로고
    • Rapid and sensitive detection of respiratory virus molecular signatures using a silver nanorod array SERS substrate
    • Shanmukh S, Jones L, Driskell J, Zhao Y, Dluhy R, and Tripp RA. Rapid and sensitive detection of respiratory virus molecular signatures using a silver nanorod array SERS substrate. Nano Lett. 2000;6:2630-2636.
    • (2000) Nano Lett. , vol.6 , pp. 2630-2636
    • Shanmukh, S.1    Jones, L.2    Driskell, J.3    Zhao, Y.4    Dluhy, R.5    Tripp, R.A.6
  • 45
    • 34547260471 scopus 로고    scopus 로고
    • Discrimination of bacteria and bacteriophages by Raman spectroscopy and surface-enhanced Raman spectroscopy
    • Goeller LJ and Riley MR. Discrimination of bacteria and bacteriophages by Raman spectroscopy and surface-enhanced Raman spectroscopy. Appl. Spectrosc. 2007;61:679-685.
    • (2007) Appl. Spectrosc. , vol.61 , pp. 679-685
    • Goeller, L.J.1    Riley, M.R.2
  • 46
    • 33749057923 scopus 로고    scopus 로고
    • Structure and behaviour of biomolecules from Raman optical activity
    • Barron LD. Structure and behaviour of biomolecules from Raman optical activity. Curr. Opin. Struct. Biol. 2006;16:638-643.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 638-643
    • Barron, L.D.1
  • 47
    • 0036802313 scopus 로고    scopus 로고
    • Protein and peptide secondary structure and conformational determination with vibrational circular dichroism
    • Keiderling TA. Protein and peptide secondary structure and conformational determination with vibrational circular dichroism. Curr. Opin. Chem. Biol. 2002;6:682-688.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 682-688
    • Keiderling, T.A.1
  • 48
    • 23044452465 scopus 로고    scopus 로고
    • Structures of plant viruses from vibrational circular dichroism
    • Shanmugam G. Polavarapu PL, Kendall A, and Stubbs G. Structures of plant viruses from vibrational circular dichroism. J. Gen. Virol. 2005;86:2371-2377.
    • (2005) J. Gen. Virol. , vol.86 , pp. 2371-2377
    • Shanmugam, G.1    Polavarapu, P.L.2    Kendall, A.3    Stubbs, G.4
  • 50
    • 32644437409 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on the physical stability of adenovirus type 5
    • Rexroad J. Evans RK, and Middaugh CR. Effect of pH and ionic strength on the physical stability of adenovirus type 5. J. Pharm. Sci. 2006;95:237-247.
    • (2006) J. Pharm. Sci. , vol.95 , pp. 237-247
    • Rexroad, J.1    Evans, R.K.2    Middaugh, C.R.3
  • 51
    • 0026516865 scopus 로고
    • Detection of proteins and phenol in DNA samples with second-derivative absorption spectroscopy
    • Mach H. Middaugh CR, and Lewis RV. Detection of proteins and phenol in DNA samples with second-derivative absorption spectroscopy. Anal. Biochem. 1992;200:20-26.
    • (1992) Anal. Biochem. , vol.200 , pp. 20-26
    • Mach, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 54
    • 0037171150 scopus 로고    scopus 로고
    • Tryptophan phosphorescence and pressure effects on protein structure
    • Cioni P and Strambini GB. Tryptophan phosphorescence and pressure effects on protein structure. Biochim. Biophys. Acta 2002;1595:116-130.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 116-130
    • Cioni, P.1    Strambini, G.B.2
  • 57
    • 44649133131 scopus 로고    scopus 로고
    • Extrinsic fluorescent dyes as tools for protein characterization
    • Hawe A. Sutter M, and Jiskoot W. Extrinsic fluorescent dyes as tools for protein characterization. Pharm. Res. 2008;25:1487-1499.
    • (2008) Pharm. Res. , vol.25 , pp. 1487-1499
    • Hawe, A.1    Sutter, M.2    Jiskoot, W.3
  • 58
    • 0037607609 scopus 로고    scopus 로고
    • A fluorescence study of the structure and accessibility of plasmid DNA condensed with cationic gene delivery vehicles
    • Wiethoff CM. Gill ML, Koe GS, Koe JG, and Middaugh CR. A fluorescence study of the structure and accessibility of plasmid DNA condensed with cationic gene delivery vehicles. J. Pharm. Sci. 2003;92:1272-1285.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 1272-1285
    • Wiethoff, C.M.1    Gill, M.L.2    Koe, G.S.3    Koe, J.G.4    Middaugh, C.R.5
  • 60
    • 53549116738 scopus 로고    scopus 로고
    • The complex inter-relationships between protein flexibility and stability
    • Kamerzell TJ. and Middaugh CR. The complex inter-relationships between protein flexibility and stability. J. Pharm. Sci. 2008;97:3494-3517.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 3494-3517
    • Kamerzell, T.J.1    Middaugh, C.R.2
  • 62
    • 0024259064 scopus 로고    scopus 로고
    • Red-edge-excitation fluorescence spectroscopy of single-tryptophan proteins
    • Demchenko AP. Red-edge-excitation fluorescence spectroscopy of single-tryptophan proteins. Eur. Biophys. J. 1998;16:121-129.
    • (1998) Eur. Biophys. J. , vol.16 , pp. 121-129
    • Demchenko, A.P.1
  • 63
    • 0036363969 scopus 로고    scopus 로고
    • The red-edge effects: 30 years of exploration
    • Demchenko AP. The red-edge effects: 30 years of exploration. Luminescence 2002;17:19-42.
    • (2002) Luminescence , vol.17 , pp. 19-42
    • Demchenko, A.P.1
  • 64
    • 38649113853 scopus 로고    scopus 로고
    • An unusual rededge excitation and time-dependent Stokes shift in the single tryptophan mutant protein DD-carboxypeptidase from Streptomyces: The role of dynamics and tryptophan rotamers
    • Maglia G. Jonckheer A, De Maeyer M, Frere JM, and Engelborghs Y. An unusual rededge excitation and time-dependent Stokes shift in the single tryptophan mutant protein DD-carboxypeptidase from Streptomyces: The role of dynamics and tryptophan rotamers. Protein Sci. 2008;17:352-361.
    • (2008) Protein Sci. , vol.17 , pp. 352-361
    • Maglia, G.1    Jonckheer, A.2    De Maeyer, M.3    Frere, J.M.4    Engelborghs, Y.5
  • 65
    • 42449118010 scopus 로고    scopus 로고
    • Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability
    • Kamerzell TJ. Ramsey JD, and Middaugh CR. Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability. J. Phys. Chem. B 2008;112:3240-3250.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3240-3250
    • Kamerzell, T.J.1    Ramsey, J.D.2    Middaugh, C.R.3
  • 66
    • 34548230395 scopus 로고    scopus 로고
    • Two-dimensional correlation spectroscopy reveals coupled immunoglobulin regions of differential flexibility that influence stability
    • Kamerzell TJ. and Middaugh CR. Two-dimensional correlation spectroscopy reveals coupled immunoglobulin regions of differential flexibility that influence stability. Biochemistry 2007;46:9762-9773.
    • (2007) Biochemistry , vol.46 , pp. 9762-9773
    • Kamerzell, T.J.1    Middaugh, C.R.2
  • 67
    • 0041336626 scopus 로고    scopus 로고
    • Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study
    • Kueltzo LA. Ersoy B, Darrington T, Ralston JP, and Middaugh CR. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study. J. Pharm. Sci. 2003;92:1805-1820.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 1805-1820
    • Kueltzo, L.A.1    Ersoy, B.2    Darrington, T.3    Ralston, J.P.4    Middaugh, C.R.5
  • 68
    • 34250703143 scopus 로고    scopus 로고
    • Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1
    • Fan H, Li H, Zhang M, and Middaugh CR. Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1. J. Pharm. Sci. 2007;96:1490-1503.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 1490-1503
    • Fan, H.1    Li, H.2    Zhang, M.3    Middaugh, C.R.4
  • 69
    • 33947538420 scopus 로고    scopus 로고
    • Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants
    • Peek LJ, Martin TT, Elk Nation C, Pegram SA, and Middaugh CR. Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants. J. Pharm. Sci. 2007;96:547-557.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 547-557
    • Peek, L.J.1    Martin, T.T.2    Elk Nation, C.3    Pegram, S.A.4    Middaugh, C.R.5
  • 70
    • 34248566786 scopus 로고    scopus 로고
    • Characterizing protein structure in amorphous solids using hydrogen/deuterium exchange with mass spectrometry
    • Li Y, Williams TD, Schowen RL, and Topp EM. Characterizing protein structure in amorphous solids using hydrogen/deuterium exchange with mass spectrometry. Anal. Biochem. 2007;366:18-28.
    • (2007) Anal. Biochem. , vol.366 , pp. 18-28
    • Li, Y.1    Williams, T.D.2    Schowen, R.L.3    Topp, E.M.4
  • 71
    • 39149141888 scopus 로고    scopus 로고
    • Effects of excipients on protein conformation in lyophilized solids by hydrogen/deuterium exchange mass spectrometry
    • Li Y, Williams TD, and Topp EM. Effects of excipients on protein conformation in lyophilized solids by hydrogen/deuterium exchange mass spectrometry. Pharm Res. 2008;25:259-267.
    • (2008) Pharm Res. , vol.25 , pp. 259-267
    • Li, Y.1    Williams, T.D.2    Topp, E.M.3
  • 73
    • 34548304719 scopus 로고    scopus 로고
    • Solution NMR of supramolecular complexes: Providing new insights into function
    • Sprangers R, Velyvis A, and Kay LE. Solution NMR of supramolecular complexes: Providing new insights into function. Nat. Methods 2007;4:697-703.
    • (2007) Nat. Methods , vol.4 , pp. 697-703
    • Sprangers, R.1    Velyvis, A.2    Kay, L.E.3
  • 74
    • 48249102645 scopus 로고    scopus 로고
    • NMR insights into a megadalton-size protein selfassembly
    • Chugh J, Sharma S, and Hosur RV. NMR insights into a megadalton-size protein selfassembly. Protein Sci. 2008;17:1319-1325.
    • (2008) Protein Sci. , vol.17 , pp. 1319-1325
    • Chugh, J.1    Sharma, S.2    Hosur, R.V.3
  • 75
    • 41849131847 scopus 로고    scopus 로고
    • Assessment of the three-dimensional structure of recombinant protein therapeutics by NMR fingerprinting: Demonstration on recombinant human granulocyte macrophage-colony stimulation factor
    • Aubin Y, Gingras G, and Sauve S. Assessment of the three-dimensional structure of recombinant protein therapeutics by NMR fingerprinting: Demonstration on recombinant human granulocyte macrophage-colony stimulation factor. Anal. Chem. 2008;80:2623-2627.
    • (2008) Anal. Chem. , vol.80 , pp. 2623-2627
    • Aubin, Y.1    Gingras, G.2    Sauve, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.