메뉴 건너뛰기




Volumn 48, Issue 2, 2013, Pages 193-204

Induction of protein conformational change inside the charged electrospray droplet

Author keywords

charge state distribution; charged droplets; conformational change; electrospray ionization; proteins

Indexed keywords

ACETIC ACID VAPOR; ANALYTE MOLECULES; ANALYTES; CHARGE STATE DISTRIBUTION; CHARGED DROPLET; CONFORMATIONAL CHANGE; ELECTROSPRAY DROPLETS; ELECTROSPRAYS; LIFE SPAN; MASS SPECTRA; MULTI-MODAL; PROTEIN MOLECULES; SOLVENT ENVIRONMENTS; STRUCTURAL FLEXIBILITIES; TIME-SCALES;

EID: 84873354333     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.3148     Document Type: Article
Times cited : (22)

References (66)
  • 1
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • J. B. Fenn, M. Mann, C. K. Meng, S. F. Wong, C. M. Whitehouse,. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246, 64.
    • (1989) Science , vol.246 , pp. 64
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 2
    • 84867456874 scopus 로고    scopus 로고
    • Electrospray Ionization Mass Spectrometry: A Technique to Access the Information beyond the Molecular Weight of the Analyte
    • DOI: 10.1155/2012/282574.
    • S. Banerjee, S. Mazumdar,. Electrospray Ionization Mass Spectrometry: A Technique to Access the Information beyond the Molecular Weight of the Analyte. Int. J. Anal. Chem. 2012. DOI: 10.1155/2012/282574.
    • (2012) Int. J. Anal. Chem.
    • Banerjee, S.1    Mazumdar, S.2
  • 3
    • 0002884477 scopus 로고    scopus 로고
    • Changes in bulk solution pH caused by the inherent controlled-current electrolytic process of an electrospray ion source
    • G. J. Van Berkel, F. Zhou, J. T. Aronson,. Changes in bulk solution pH caused by the inherent controlled-current electrolytic process of an electrospray ion source. Int. J. Mass Spectrom. Ion Processes 1997, 162, 55.
    • (1997) Int. J. Mass Spectrom. Ion Processes , vol.162 , pp. 55
    • Van Berkel, G.J.1    Zhou, F.2    Aronson, J.T.3
  • 4
    • 0033557548 scopus 로고    scopus 로고
    • Investigation of the Electrospray Plume by Laser-Induced Fluorescence Spectroscopy
    • S. Zhou, A. G. Edwards, K. D. Cook, G. J. Van Berkel,. Investigation of the Electrospray Plume by Laser-Induced Fluorescence Spectroscopy. Anal. Chem. 1999, 71, 769.
    • (1999) Anal. Chem. , vol.71 , pp. 769
    • Zhou, S.1    Edwards, A.G.2    Cook, K.D.3    Van Berkel, G.J.4
  • 5
    • 12044253267 scopus 로고
    • From ions in solution to ions in the gas phase - The mechanism of electrospray mass spectrometry
    • P. Kebarle, L. Tang,. From ions in solution to ions in the gas phase-the mechanism of electrospray mass spectrometry. Anal. Chem. 1993, 65, 972A.
    • (1993) Anal. Chem. , vol.65
    • Kebarle, P.1    Tang, L.2
  • 6
    • 0000863112 scopus 로고
    • Acidity Determination in Droplets Formed by Electrospraying Methanol-Water Solutions
    • C. L. Gatlin, F. Turecek,. Acidity Determination in Droplets Formed by Electrospraying Methanol-Water Solutions. Anal. Chem. 1994, 66, 712.
    • (1994) Anal. Chem. , vol.66 , pp. 712
    • Gatlin, C.L.1    Turecek, F.2
  • 7
    • 80755159123 scopus 로고    scopus 로고
    • Evidence of Molecular Fragmentation inside the Charged Droplets Produced by Electrospray Process
    • S. Banerjee, H. Prakash, S. Mazumdar,. Evidence of Molecular Fragmentation inside the Charged Droplets Produced by Electrospray Process. J. Am. Soc. Mass Spectrom. 2011, 22, 1707.
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1707
    • Banerjee, S.1    Prakash, H.2    Mazumdar, S.3
  • 8
    • 0037466992 scopus 로고    scopus 로고
    • Mechanism of charging and supercharging molecules in electrospray ionization
    • A. T. Iavarone, E. R. Williams,. Mechanism of charging and supercharging molecules in electrospray ionization. J. Am. Chem. Soc. 2003, 125, 2319.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2319
    • Iavarone, A.T.1    Williams, E.R.2
  • 9
    • 0001510590 scopus 로고
    • Ion formation from charged droplets: Roles of geometry, energy, and time
    • J. B. Fenn,. Ion formation from charged droplets: roles of geometry, energy, and time. J. Am. Soc. Mass Spectrom. 1993, 4, 524.
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 524
    • Fenn, J.B.1
  • 11
    • 57449113443 scopus 로고    scopus 로고
    • Stepwise evolution of protein native structure with electrospray into the gas phase, 10(-12) to 10(2) s
    • K. Breuker, F. W. McLafferty,. Stepwise evolution of protein native structure with electrospray into the gas phase, 10(-12) to 10(2) s. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 18145.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18145
    • Breuker, K.1    McLafferty, F.W.2
  • 12
    • 77956253029 scopus 로고    scopus 로고
    • Electrospray Droplet Exposure to Gaseous Acids for the Manipulation of Protein Charge State Distributions
    • A. Kharlamova, B. M. Prentice, T.-Y. Huang, S. A. McLuckey,. Electrospray Droplet Exposure to Gaseous Acids for the Manipulation of Protein Charge State Distributions. Anal. Chem. 2010, 82, 7422.
    • (2010) Anal. Chem. , vol.82 , pp. 7422
    • Kharlamova, A.1    Prentice, B.M.2    Huang, T.-Y.3    McLuckey, S.A.4
  • 13
    • 78650776668 scopus 로고    scopus 로고
    • Negative Electrospray Droplet Exposure to Gaseous Bases for the Manipulation of Protein Charge State Distributions
    • A. Kharlamova, S. A. McLuckey,. Negative Electrospray Droplet Exposure to Gaseous Bases for the Manipulation of Protein Charge State Distributions. Anal. Chem. 2011, 83, 431.
    • (2011) Anal. Chem. , vol.83 , pp. 431
    • Kharlamova, A.1    McLuckey, S.A.2
  • 14
    • 77949386262 scopus 로고    scopus 로고
    • Tuning the substrate specificity by engineering the active site of cytochrome P450cam: A rational approach
    • S. K. Manna, S. Mazumdar,. Tuning the substrate specificity by engineering the active site of cytochrome P450cam: A rational approach. Dalton Trans. 2010, 39, 3115.
    • (2010) Dalton Trans. , vol.39 , pp. 3115
    • Manna, S.K.1    Mazumdar, S.2
  • 16
    • 79958236206 scopus 로고    scopus 로고
    • Reduced Fluorescence Lifetime Heterogeneity of 5-Fluorotryptophan in Comparison to Tryptophan in Proteins: Implication for Resonance Energy Transfer Experiments
    • S. S. Sarkar, J. B. Udgaonkar, G. Krishnamoorthy,. Reduced Fluorescence Lifetime Heterogeneity of 5-Fluorotryptophan in Comparison to Tryptophan in Proteins: Implication for Resonance Energy Transfer Experiments. J. Phys. Chem. B 2011, 115, 7479.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7479
    • Sarkar, S.S.1    Udgaonkar, J.B.2    Krishnamoorthy, G.3
  • 18
    • 33947482089 scopus 로고
    • Dithiothreitol, a New Protective Reagent for SH Groups
    • W. W. Cleland,. Dithiothreitol, a New Protective Reagent for SH Groups. Biochemistry 1964, 3, 480.
    • (1964) Biochemistry , vol.3 , pp. 480
    • Cleland, W.W.1
  • 19
    • 78650839196 scopus 로고    scopus 로고
    • Non-covalent dimers of the lysine containing protonated peptide ions in gaseous state: Electrospray ionization mass spectrometric study
    • S. Banerjee, S. Mazumdar,. Non-covalent dimers of the lysine containing protonated peptide ions in gaseous state: electrospray ionization mass spectrometric study. J. Mass Spectrom. 2010, 45, 1212.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 1212
    • Banerjee, S.1    Mazumdar, S.2
  • 20
    • 23844469161 scopus 로고    scopus 로고
    • Direct correlation of the crystal structure of proteins with the maximum positive and negative charge states of gaseous protein ions produced by electrospray ionization
    • H. Prakash, S. Mazumdar,. Direct correlation of the crystal structure of proteins with the maximum positive and negative charge states of gaseous protein ions produced by electrospray ionization. J. Am. Soc. Mass Spectrom. 2005, 16, 1409.
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 1409
    • Prakash, H.1    Mazumdar, S.2
  • 21
    • 72249101959 scopus 로고    scopus 로고
    • Effects of salts on the charge-state distribution and the structural basis of the most-intense charge-state of the gaseous protein ions produced by electrospray ionization
    • H. Prakash, B. T. Kansara, S. Mazumdar,. Effects of salts on the charge-state distribution and the structural basis of the most-intense charge-state of the gaseous protein ions produced by electrospray ionization. Int. J. Mass Spectrom. 2010, 289, 84.
    • (2010) Int. J. Mass Spectrom. , vol.289 , pp. 84
    • Prakash, H.1    Kansara, B.T.2    Mazumdar, S.3
  • 22
    • 59349106621 scopus 로고    scopus 로고
    • Succinylation of cytochrome c investigated by electrospray ionization mass spectrometry: Reactive lysine residues
    • H. Prakash, S. Mazumdar,. Succinylation of cytochrome c investigated by electrospray ionization mass spectrometry: Reactive lysine residues. Int. J. Mass Spectrom. 2009, 281, 55.
    • (2009) Int. J. Mass Spectrom. , vol.281 , pp. 55
    • Prakash, H.1    Mazumdar, S.2
  • 23
    • 4244120329 scopus 로고
    • Effect of Solution Ionic Strength on Analyte Charge State Distributions in Positive and Negative Ion Electrospray Mass Spectrometry
    • G. Wang, R. B. Cole,. Effect of Solution Ionic Strength on Analyte Charge State Distributions in Positive and Negative Ion Electrospray Mass Spectrometry. Anal. Chem. 1994, 66, 3702.
    • (1994) Anal. Chem. , vol.66 , pp. 3702
    • Wang, G.1    Cole, R.B.2
  • 25
    • 36749115028 scopus 로고
    • On the evaporation of small ions from charged droplets
    • J. V. Iribarne, B. A. Thomson,. On the evaporation of small ions from charged droplets. J. Chem. Phys. 1976, 64, 2287.
    • (1976) J. Chem. Phys. , vol.64 , pp. 2287
    • Iribarne, J.V.1    Thomson, B.A.2
  • 26
  • 27
    • 0002124332 scopus 로고    scopus 로고
    • Electrospray ionization of large multiply charged species proceeds via Dole's charged residue mechanism
    • J. Fernandez de la Mora,. Electrospray ionization of large multiply charged species proceeds via Dole's charged residue mechanism. Anal. Chim. Acta 2000, 406, 93.
    • (2000) Anal. Chim. Acta , vol.406 , pp. 93
    • Fernandez De La Mora, J.1
  • 28
    • 0033957354 scopus 로고    scopus 로고
    • On the mechanisms by which the charged droplets produced by electrospray lead to gas phase ions
    • P. Kebarle, M. Peschke,. On the mechanisms by which the charged droplets produced by electrospray lead to gas phase ions. Anal. Chim. Acta 2000, 406, 11.
    • (2000) Anal. Chim. Acta , vol.406 , pp. 11
    • Kebarle, P.1    Peschke, M.2
  • 29
    • 0000547607 scopus 로고
    • Electrospray analysis of proteins: A comparison of positive-ion and negative-ion mass spectra at high and low pH
    • M. A. Kelly, M. M. Vestling, C. C. Fenselau, P. B. Smith,. Electrospray analysis of proteins: A comparison of positive-ion and negative-ion mass spectra at high and low pH. Org. Mass Spectrom. 1992, 27, 1143.
    • (1992) Org. Mass Spectrom. , vol.27 , pp. 1143
    • Kelly, M.A.1    Vestling, M.M.2    Fenselau, C.C.3    Smith, P.B.4
  • 31
    • 0031082985 scopus 로고    scopus 로고
    • Ion-molecule reactions as probes of gas-phase structures of peptides and proteins
    • M. K. Green, C. B. Lebrilla,. Ion-molecule reactions as probes of gas-phase structures of peptides and proteins. Mass Spectrom. Rev. 1997, 16, 53.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 53
    • Green, M.K.1    Lebrilla, C.B.2
  • 32
    • 0035298817 scopus 로고    scopus 로고
    • Supercharged Protein and Peptide Ions Formed by Electrospray Ionization
    • A. T. Iavarone, J. C. Jurchen, E. R. Williams,. Supercharged Protein and Peptide Ions Formed by Electrospray Ionization. Anal. Chem. 2001, 73, 1455.
    • (2001) Anal. Chem. , vol.73 , pp. 1455
    • Iavarone, A.T.1    Jurchen, J.C.2    Williams, E.R.3
  • 34
    • 0001093176 scopus 로고
    • On the equilibrium of liquid conducting masses charged with electricity
    • L. Rayleigh,. On the equilibrium of liquid conducting masses charged with electricity. Philos. Mag. 1882, 14, 184.
    • (1882) Philos. Mag. , vol.14 , pp. 184
    • Rayleigh, L.1
  • 37
    • 0030827122 scopus 로고    scopus 로고
    • Acid-Induced Unfolding of Cytochrome c at Different Methanol Concentrations: Electrospray Ionization Mass Spectrometry Specifically Monitors Changes in the Tertiary Structure
    • L. Konermann, D. J. Douglas,. Acid-Induced Unfolding of Cytochrome c at Different Methanol Concentrations: Electrospray Ionization Mass Spectrometry Specifically Monitors Changes in the Tertiary Structure. Biochemistry 1997, 36, 12296.
    • (1997) Biochemistry , vol.36 , pp. 12296
    • Konermann, L.1    Douglas, D.J.2
  • 38
    • 0032232233 scopus 로고    scopus 로고
    • Unfolding of proteins monitored by electrospray ionization mass spectrometry: A comparison of positive and negative ion modes
    • L. Konermann, D. J. Douglas,. Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes. J. Am. Soc. Mass Spectrom. 1998, 9, 1248.
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 1248
    • Konermann, L.1    Douglas, D.J.2
  • 39
    • 0025674590 scopus 로고
    • Probing conformational changes in proteins by mass spectrometry
    • S. K. Chowdhury, V. Katta, B. T. Chait,. Probing conformational changes in proteins by mass spectrometry. J. Am. Chem. Soc. 1990, 112, 9012.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9012
    • Chowdhury, S.K.1    Katta, V.2    Chait, B.T.3
  • 40
    • 64049085647 scopus 로고    scopus 로고
    • Irreversible Thermal Denaturation of Cytochrome c Studied by Electrospray Mass Spectrometry
    • J. Liu, L. Konermann,. Irreversible Thermal Denaturation of Cytochrome c Studied by Electrospray Mass Spectrometry. J. Am. Soc. Mass Spectrom. 2009, 20, 819.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 819
    • Liu, J.1    Konermann, L.2
  • 41
    • 23744516059 scopus 로고    scopus 로고
    • Estimates of protein surface areas in solution by electrospray ionization mass spectrometry
    • I. A. Kaltashov, A. Mohimen,. Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Anal. Chem. 2005, 77, 5370.
    • (2005) Anal. Chem. , vol.77 , pp. 5370
    • Kaltashov, I.A.1    Mohimen, A.2
  • 42
    • 50849098485 scopus 로고    scopus 로고
    • Do Ionic Charges in ESI MS Provide Useful Information on Macromolecular Structure?
    • I. A. Kaltashov, R. R. Abzalimov,. Do Ionic Charges in ESI MS Provide Useful Information on Macromolecular Structure? J. Am. Soc. Mass Spectrom. 2008, 19, 1239.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1239
    • Kaltashov, I.A.1    Abzalimov, R.R.2
  • 43
    • 70349136225 scopus 로고    scopus 로고
    • Origin of Supercharging in Electrospray Ionization of Noncovalent Complexes from Aqueous Solution
    • H. J. Sterling, E. R. Williams,. Origin of Supercharging in Electrospray Ionization of Noncovalent Complexes from Aqueous Solution. J. Am. Soc. Mass Spectrom. 2009, 20, 1933.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1933
    • Sterling, H.J.1    Williams, E.R.2
  • 47
    • 84990438778 scopus 로고
    • Physical properties of matrices used for fast atom bombardment
    • K. D. Cook, P. J. Todd, D. H. Friar,. Physical properties of matrices used for fast atom bombardment. Biol. Mass Spectrom. 1989, 18, 492.
    • (1989) Biol. Mass Spectrom. , vol.18 , pp. 492
    • Cook, K.D.1    Todd, P.J.2    Friar, D.H.3
  • 48
    • 0017349738 scopus 로고
    • Structure of myoglobin refined at 2 · 0 A resolution: II. Structure of deoxymyoglobin from sperm whale
    • T. Takano,. Structure of myoglobin refined at 2 · 0 A resolution: II. Structure of deoxymyoglobin from sperm whale. J. Mol. Biol. 1977, 110, 569.
    • (1977) J. Mol. Biol. , vol.110 , pp. 569
    • Takano, T.1
  • 49
    • 0034487655 scopus 로고    scopus 로고
    • Effects of solvent on the maximum charge state and charge state distribution of protein ions produced by electrospray ionization
    • A. T. Iavarone, J. C. Jurchen, E. R. Williams,. Effects of solvent on the maximum charge state and charge state distribution of protein ions produced by electrospray ionization. J. Am. Soc. Mass Spectrom. 2000, 11, 976.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 976
    • Iavarone, A.T.1    Jurchen, J.C.2    Williams, E.R.3
  • 50
    • 18344365407 scopus 로고    scopus 로고
    • Testing the role of solvent surface tension in protein ionization by electrospray
    • M. Šamalikova, R. Grandori,. Testing the role of solvent surface tension in protein ionization by electrospray. J. Mass Spectrom. 2005, 40, 503.
    • (2005) J. Mass Spectrom. , vol.40 , pp. 503
    • Šamalikova, M.1    Grandori, R.2
  • 51
    • 0030919476 scopus 로고    scopus 로고
    • Acid-Induced Denaturation of Myoglobin Studied by Time-Resolved Electrospray Ionization Mass Spectrometry
    • L. Konermann, F. I. Rosell, A. G. Mauk, D. J. Douglas,. Acid-Induced Denaturation of Myoglobin Studied by Time-Resolved Electrospray Ionization Mass Spectrometry. Biochemistry 1997, 36, 6448.
    • (1997) Biochemistry , vol.36 , pp. 6448
    • Konermann, L.1    Rosell, F.I.2    Mauk, A.G.3    Douglas, D.J.4
  • 53
    • 34249679399 scopus 로고    scopus 로고
    • Conformational Changes of Proteins Observed by Hydrogen/Deuterium Exchange and Electrospray Ionization Mass Spectrometry
    • S. Akashi, K. Takio,. Conformational Changes of Proteins Observed by Hydrogen/Deuterium Exchange and Electrospray Ionization Mass Spectrometry. J. Mass Spectrom. Soc. Japan 1998, 46, 75.
    • (1998) J. Mass Spectrom. Soc. Japan , vol.46 , pp. 75
    • Akashi, S.1    Takio, K.2
  • 54
    • 0013852463 scopus 로고
    • Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 [angst] Resolution
    • C. C. F. Blake, D. F. Koenig, G. A. Mair, A. C. T. North, D. C. Phillips, V. R. Sarma,. Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 [angst] Resolution. Nature 1965, 206, 757.
    • (1965) Nature , vol.206 , pp. 757
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 55
    • 0023473677 scopus 로고
    • Mechanism and Stereoelectronic Effects in the Lysozyme Reactio
    • A. J. Kirby,. Mechanism and Stereoelectronic Effects in the Lysozyme Reactio. Crit. Rev. Biochem. Mol. Biol. 1987, 22, 283.
    • (1987) Crit. Rev. Biochem. Mol. Biol. , vol.22 , pp. 283
    • Kirby, A.J.1
  • 56
    • 0015221360 scopus 로고
    • Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozyme
    • C. C. McDonald, W. D. Phillips, J. D. Glickson,. Nuclear magnetic resonance study of the mechanism of reversible denaturation of lysozyme. J. Am. Chem. Soc. 1971, 93, 235.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 235
    • McDonald, C.C.1    Phillips, W.D.2    Glickson, J.D.3
  • 57
    • 0029953934 scopus 로고    scopus 로고
    • Stabilization of Barstar by Chemical Modification of the Buried Cysteines
    • S. Ramachandran, J. B. Udgaonkar,. Stabilization of Barstar by Chemical Modification of the Buried Cysteines. Biochemistry 1996, 35, 8776.
    • (1996) Biochemistry , vol.35 , pp. 8776
    • Ramachandran, S.1    Udgaonkar, J.B.2
  • 58
    • 9344227330 scopus 로고    scopus 로고
    • Native and nonnative conformational preferences in the urea-unfolded state of barstar
    • N. S. Bhavesh, J. Juneja, J. B. Udgaonkar, R. V. Hosur,. Native and nonnative conformational preferences in the urea-unfolded state of barstar. Protein Sci. 2004, 13, 3085.
    • (2004) Protein Sci. , vol.13 , pp. 3085
    • Bhavesh, N.S.1    Juneja, J.2    Udgaonkar, J.B.3    Hosur, R.V.4
  • 59
    • 0028901085 scopus 로고
    • The Folding Mechanism of Barstar: Evidence for Multiple Pathways and Multiple Intermediates
    • M. C. R. Shastry, J. B. Udgaonkar,. The Folding Mechanism of Barstar: Evidence for Multiple Pathways and Multiple Intermediates. J. Mol. Biol. 1995, 247, 1013.
    • (1995) J. Mol. Biol. , vol.247 , pp. 1013
    • Shastry, M.C.R.1    Udgaonkar, J.B.2
  • 61
    • 0034683158 scopus 로고    scopus 로고
    • An Experimental and Ab Initio Study of the Nature of the Binding in Gas-Phase Complexes of Sodium Ions
    • T. B. McMahon, G. Ohanessian,. An Experimental and Ab Initio Study of the Nature of the Binding in Gas-Phase Complexes of Sodium Ions. Chem. Eur. J. 2000, 6, 2931.
    • (2000) Chem. Eur. J. , vol.6 , pp. 2931
    • McMahon, T.B.1    Ohanessian, G.2
  • 63
    • 0033551171 scopus 로고    scopus 로고
    • A Refined Model for the Solution Structure of Oxidized Putidaredoxin
    • T. C. Pochapsky, N. U. Jain, M. Kuti, T. A. Lyons, J. Heymont,. A Refined Model for the Solution Structure of Oxidized Putidaredoxin. Biochemistry 1999, 38, 4681.
    • (1999) Biochemistry , vol.38 , pp. 4681
    • Pochapsky, T.C.1    Jain, N.U.2    Kuti, M.3    Lyons, T.A.4    Heymont, J.5
  • 64
    • 0030457189 scopus 로고    scopus 로고
    • A structure-based model for cytochrome P450cam-putidaredoxin interactions
    • T. C. Pochapsky, T. A. Lyons, S. Kazanis, T. Arakaki, G. Ratnaswamy,. A structure-based model for cytochrome P450cam-putidaredoxin interactions. Biochimie 1996, 78, 723.
    • (1996) Biochimie , vol.78 , pp. 723
    • Pochapsky, T.C.1    Lyons, T.A.2    Kazanis, S.3    Arakaki, T.4    Ratnaswamy, G.5
  • 66
    • 84858646967 scopus 로고    scopus 로고
    • Profiling an electrospray plume by laser-induced fluorescence and Fraunhofer diffraction combined to mass spectrometry: Influence of size and composition of droplets on charge-state distributions of electrosprayed proteins
    • M. Girod, X. Dagany, V. Boutou, M. Broyer, R. Antoine, P. Dugourd, A. Mordehai, C. Love, M. Werlich, J. Fjeldsted, G. Stafford,. Profiling an electrospray plume by laser-induced fluorescence and Fraunhofer diffraction combined to mass spectrometry: influence of size and composition of droplets on charge-state distributions of electrosprayed proteins. Phys. Chem. Chem. Phys. 2012, 14, 9389.
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 9389
    • Girod, M.1    Dagany, X.2    Boutou, V.3    Broyer, M.4    Antoine, R.5    Dugourd, P.6    Mordehai, A.7    Love, C.8    Werlich, M.9    Fjeldsted, J.10    Stafford, G.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.