메뉴 건너뛰기




Volumn 26, Issue 1, 2014, Pages 71-82

Time-resolved pulsed hydrogen/deuterium exchange mass spectrometry probes gaseous proteins structural kinetics

Author keywords

Continuum gas flow; Electrospray ionization (ESI) MS; Gas phase HDX kinetics; Ion molecule reactions; Isotopic labeling; Protein; Pulsed hydrogen deuterium exchange mass spectrometry (HDX MS); Time of flight mass spectrometry (TOF MS); Time resolved structural analysis

Indexed keywords

ELECTROSPRAY IONIZATION; FLOW OF GASES; GASES; HYDROGEN; ION EXCHANGE; IONIZATION OF GASES; IONS; KINETICS; MASS SPECTROMETRY;

EID: 84919950774     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-014-1004-y     Document Type: Article
Times cited : (4)

References (58)
  • 1
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • 1:CAS:528:DC%2BD28Xht12gs7k%3D 10.1002/mas.20064
    • Wales, T.E.; Engen, J.R.: Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170 (2006)
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 2
    • 84863207545 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: Are we out of the quicksand?
    • 1:CAS:528:DC%2BC38Xms1Witb4%3D 10.1007/s13361-012-0377-z
    • Iacob, R.E.; Engen, J.R.: Hydrogen exchange mass spectrometry: are we out of the quicksand? J. Am. Soc. Mass Spectrom. 23, 1003-1010 (2012)
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1003-1010
    • Iacob, R.E.1    Engen, J.R.2
  • 3
    • 84862014667 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry for monitoring millisecond time-scale solution-phase processes
    • 1:CAS:528:DC%2BC38Xpt1ertro%3D 10.1255/ejms.1176
    • Rob, T.; Wilson, D.J.: Time-resolved mass spectrometry for monitoring millisecond time-scale solution-phase processes. Eur. J. Mass Spectrom. 18, 205-214 (2012)
    • (2012) Eur. J. Mass Spectrom. , vol.18 , pp. 205-214
    • Rob, T.1    Wilson, D.J.2
  • 4
    • 0032013052 scopus 로고    scopus 로고
    • Local structure and dynamics in proteins characterized by hydrogen exchange and mass spectrometry
    • 1:CAS:528:DyaK1cXjs1Sgsro%3D
    • Smith, D.L.: Local structure and dynamics in proteins characterized by hydrogen exchange and mass spectrometry. Biokhimiia 63, 285-293 (1998)
    • (1998) Biokhimiia , vol.63 , pp. 285-293
    • Smith, D.L.1
  • 6
    • 65249153623 scopus 로고    scopus 로고
    • Characterization of nucleic acid higher order structure by gas-phase H/D exchange in a quadrupole-FT-ICR mass spectrometer
    • 1:CAS:528:DC%2BD1MXivVaru7s%3D 10.1002/bip.21134
    • Mo, J.; Todd, G.C.; Håkansson, K.J.: Characterization of nucleic acid higher order structure by gas-phase H/D exchange in a quadrupole-FT-ICR mass spectrometer. Biopolymers 91, 256-264 (2009)
    • (2009) Biopolymers , vol.91 , pp. 256-264
    • Mo, J.1    Todd, G.C.2    Håkansson, K.J.3
  • 7
    • 0033976877 scopus 로고    scopus 로고
    • Enhanced gas-phase hydrogen-deuterium exchange of oligonucleotide and protein ions stored in an external multipole ion reservoir
    • 1:CAS:528:DC%2BD3cXhtVansLw%3D 10.1002/(SICI)1096-9888(200001)35:1<62: AID-JMS913>3.0.CO;2-9
    • Hofstadler, S.A.; Sannes-Lowery, K.A.; Griffey, R.H.: Enhanced gas-phase hydrogen-deuterium exchange of oligonucleotide and protein ions stored in an external multipole ion reservoir. J. Mass Spectrom. 35, 62-70 (2000)
    • (2000) J. Mass Spectrom. , vol.35 , pp. 62-70
    • Hofstadler, S.A.1    Sannes-Lowery, K.A.2    Griffey, R.H.3
  • 9
    • 0012757921 scopus 로고    scopus 로고
    • H/D exchange of gas phase bradykinin ions in a linear quadrupole ion trap
    • 1:CAS:528:DC%2BD3sXhtFClu78%3D 10.1016/S1044-0305(02)00818-8
    • Mao, D.; Douglas, D.J.: H/D exchange of gas phase bradykinin ions in a linear quadrupole ion trap. J. Am. Soc. Mass Spectrom. 14, 85-94 (2003)
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 85-94
    • Mao, D.1    Douglas, D.J.2
  • 10
    • 0030901492 scopus 로고    scopus 로고
    • Gas phase hydrogen/deuterium exchange reactions of peptide ions in a quadrupole ion trap mass spectrometer
    • 1:CAS:528:DyaK2sXjtVKltr0%3D 10.1002/(SICI)1097-0134(199705)28:1<53: AID-PROT5>3.0.CO;2-K
    • Kaltashov, I.A.; Doroshenko, V.M.; Cotter, R.J.: Gas phase hydrogen/deuterium exchange reactions of peptide ions in a quadrupole ion trap mass spectrometer. Proteins 28, 53-58 (1997)
    • (1997) Proteins , vol.28 , pp. 53-58
    • Kaltashov, I.A.1    Doroshenko, V.M.2    Cotter, R.J.3
  • 12
    • 79952236574 scopus 로고    scopus 로고
    • Gas-phase H/D-exchange experiments in supramolecular chemistry
    • 1:CAS:528:DC%2BC3MXisFKisr4%3D 10.1039/c0nj00634c
    • Winkler, H.D.F.; Dzyuba, E.V.; Schalley, C.A.: Gas-phase H/D-exchange experiments in supramolecular chemistry. New J. Chem. 35, 529-541 (2011)
    • (2011) New J. Chem. , vol.35 , pp. 529-541
    • Winkler, H.D.F.1    Dzyuba, E.V.2    Schalley, C.A.3
  • 13
    • 23844442205 scopus 로고    scopus 로고
    • Evidence for unfolding and refolding of gas-phase cytochrome c ions in a Paul trap
    • 1:CAS:528:DC%2BD2MXpt1Wmsrw%3D 10.1016/j.jasms.2005.04.013
    • Badman, E.R.; Myung, S.; Clemmer, D.E.: Evidence for unfolding and refolding of gas-phase cytochrome c ions in a Paul trap. J. Am. Soc. Mass Spectrom. 16, 1493-1497 (2005)
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 1493-1497
    • Badman, E.R.1    Myung, S.2    Clemmer, D.E.3
  • 14
    • 0035894045 scopus 로고    scopus 로고
    • Monitoring structural changes of proteins in an ion trap over ~10-200 ms: Unfolding transitions in cytochrome c ions
    • 1:CAS:528:DC%2BD3MXotFels7o%3D 10.1021/ac010744a
    • Badman, E.R.; Hoaglund-Hyzer, C.S.; Clemmer, D.E.: Monitoring structural changes of proteins in an ion trap over ~10-200 ms: unfolding transitions in cytochrome c ions. Anal. Chem. 73, 6000-6007 (2001)
    • (2001) Anal. Chem. , vol.73 , pp. 6000-6007
    • Badman, E.R.1    Hoaglund-Hyzer, C.S.2    Clemmer, D.E.3
  • 16
    • 54349118212 scopus 로고    scopus 로고
    • Early structural evolution of native cytochrome c after solvent removal
    • 1:CAS:528:DC%2BD1cXht12hsr3F
    • Steinberg, M.Z.; Elber, R.; McLafferty, F.W.; Gerber, R.B.; Breuker, K.: Early structural evolution of native cytochrome c after solvent removal. Chem. Biochem. 9, 2417-2423 (2008)
    • (2008) Chem. Biochem. , vol.9 , pp. 2417-2423
    • Steinberg, M.Z.1    Elber, R.2    McLafferty, F.W.3    Gerber, R.B.4    Breuker, K.5
  • 17
    • 0031007307 scopus 로고    scopus 로고
    • Cytochrome c folding kinetics studied by time-resolved electrospray ionization mass spectrometry
    • 1:CAS:528:DyaK2sXisFCjtrw%3D 10.1021/bi970046d
    • Konermann, L.; Collings, B.A.; Douglas, D.J.: Cytochrome c folding kinetics studied by time-resolved electrospray ionization mass spectrometry. Biochemistry 36, 5554-5559 (1997)
    • (1997) Biochemistry , vol.36 , pp. 5554-5559
    • Konermann, L.1    Collings, B.A.2    Douglas, D.J.3
  • 18
    • 0030919476 scopus 로고    scopus 로고
    • Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry
    • 1:CAS:528:DyaK2sXivF2ntL4%3D 10.1021/bi970353j
    • Konermann, L.; Rosell, F.I.; Mauk, A.G.; Douglas, D.J.: Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry. Biochemistry 36, 6448-6454 (1997)
    • (1997) Biochemistry , vol.36 , pp. 6448-6454
    • Konermann, L.1    Rosell, F.I.2    Mauk, A.G.3    Douglas, D.J.4
  • 19
    • 2442637587 scopus 로고    scopus 로고
    • 3: Exchange kinetics do not reflect parent ion structures
    • 1:CAS:528:DC%2BD2cXjsVOhsbs%3D 10.1021/ja049834y
    • 3: exchange kinetics do not reflect parent ion structures. J. Am. Chem. Soc. 126, 6485-6490 (2004)
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6485-6490
    • Cox, H.A.1    Julian, R.R.2    Lee, S.W.3    Beauchamp, J.L.4
  • 20
    • 0037168359 scopus 로고    scopus 로고
    • Structural transitions of electrosprayed ubiquitin ions stored in an ion trap over ~10 ms to 30 s
    • 1:CAS:528:DC%2BD38XmtFSrtro%3D 10.1021/jp0206368
    • Myung, S.; Badman, E.R.; Lee, Y.J.; Clemmer, D.E.: Structural transitions of electrosprayed ubiquitin ions stored in an ion trap over ~10 ms to 30 s. J. Phys. Chem. A 106, 9976-9982 (2002)
    • (2002) J. Phys. Chem. A , vol.106 , pp. 9976-9982
    • Myung, S.1    Badman, E.R.2    Lee, Y.J.3    Clemmer, D.E.4
  • 21
    • 0001676702 scopus 로고    scopus 로고
    • Gas-phase bovine ubiquitin cation conformations resolved by gas-phase hydrogen/deuterium exchange rate and extent
    • 1:CAS:528:DyaK1MXivVCktLY%3D 10.1016/S1387-3806(98)14172-6
    • Freitas, M.; Marshall, A.G.: Gas-phase bovine ubiquitin cation conformations resolved by gas-phase hydrogen/deuterium exchange rate and extent. Int. J. Mass Spectrom. 185/186/187, 565-575 (1999)
    • (1999) Int. J. Mass Spectrom. , vol.185-186 , Issue.187 , pp. 565-575
    • Freitas, M.1    Marshall, A.G.2
  • 22
    • 72449155492 scopus 로고    scopus 로고
    • Gas-phase hydrogen/deuterium exchange in a traveling wave ion guide for the examination of protein conformations
    • 1:CAS:528:DC%2BD1MXhsVeis7zL 10.1021/ac901897x
    • Rand, K.D.; Pringle, S.D.; Murphy III, J.P.; Fadgen, K.E.; Brown, J.; Engen, J.R.: Gas-phase hydrogen/deuterium exchange in a traveling wave ion guide for the examination of protein conformations. Anal. Chem. 81, 10019-10028 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 10019-10028
    • Rand, K.D.1    Pringle, S.D.2    Murphy, J.P.3    Fadgen, K.E.4    Brown, J.5    Engen, J.R.6
  • 23
    • 84863346540 scopus 로고    scopus 로고
    • Site-specific analysis of gas-phase hydrogen/deuterium exchange of peptides and proteins by electron transfer dissociation
    • 1:CAS:528:DC%2BC38XlsVGnsg%3D%3D 10.1021/ac202918j
    • Rand, K.D.; Pringle, S.D.; Morris, M.; Brown, J.M.: Site-specific analysis of gas-phase hydrogen/deuterium exchange of peptides and proteins by electron transfer dissociation. Anal. Chem. 84, 1931-1940 (2012)
    • (2012) Anal. Chem. , vol.84 , pp. 1931-1940
    • Rand, K.D.1    Pringle, S.D.2    Morris, M.3    Brown, J.M.4
  • 24
    • 0031239739 scopus 로고    scopus 로고
    • Conformer-dependent proton-transfer reactions of ubiquitin ions
    • 1:CAS:528:DyaK2sXlsFKktrc%3D 10.1016/S1044-0305(97)00085-8
    • Valentine, S.J.; Counterman, A.E.; Clemmer, D.E.: Conformer-dependent proton-transfer reactions of ubiquitin ions. J. Am. Soc. Mass Spectrom. 8, 954-961 (1997)
    • (1997) J. Am. Soc. Mass Spectrom. , vol.8 , pp. 954-961
    • Valentine, S.J.1    Counterman, A.E.2    Clemmer, D.E.3
  • 25
    • 0029664917 scopus 로고    scopus 로고
    • l2+ ions produced by electrospray ionization mass spectrometry
    • 1:CAS:528:DyaK28Xhs1CltLk%3D 10.1002/(SICI)1096-9888(199603)31:3<247: AID-JMS285>3.0.CO;2-L
    • l2+ ions produced by electrospray ionization mass spectrometry. J. Mass Spectrom. 31, 247-254 (1996)
    • (1996) J. Mass Spectrom. , vol.31 , pp. 247-254
    • Cassady, C.J.1    Carr, S.R.2
  • 27
    • 23844466290 scopus 로고    scopus 로고
    • Multidimensional separations of ubiquitin conformers in the gas phase: Relating ion cross sections to H/D exchange measurements
    • 1:CAS:528:DC%2BD2MXpt1Wnur0%3D 10.1016/j.jasms.2005.04.007
    • Robinson, E.W.; Williams, E.R.: Multidimensional separations of ubiquitin conformers in the gas phase: relating ion cross sections to H/D exchange measurements. J. Am. Soc. Mass Spectrom. 16, 1427-1437 (2005)
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 1427-1437
    • Robinson, E.W.1    Williams, E.R.2
  • 28
    • 56949107361 scopus 로고    scopus 로고
    • Conformations of gas-phase ions of ubiquitin, cytochrome c, apomyoglobin, and β-lactoglobulin produced from two different solution conformations
    • 1:CAS:528:DC%2BD1cXhsVyrtrbM 10.1016/j.jasms.2008.07.018
    • Wright, P.J.; Zhang, J.; Douglas, D.J.: Conformations of gas-phase ions of ubiquitin, cytochrome c, apomyoglobin, and β-lactoglobulin produced from two different solution conformations. J. Am. Soc. Mass Spectrom. 19, 1906-1913 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1906-1913
    • Wright, P.J.1    Zhang, J.2    Douglas, D.J.3
  • 31
    • 0031763316 scopus 로고    scopus 로고
    • A new linear ion trap time-of-flight system with tandem mass spectrometry capabilities
    • 1:CAS:528:DyaK1cXmvFOls78%3D 10.1002/(SICI)1097-0231(19981030)12:20<1463: AID-RCM357>3.0.CO;2-H
    • Campbell, J.M.; Collings, B.A.; Douglas, D.J.: A new linear ion trap time-of-flight system with tandem mass spectrometry capabilities. Rapid Commun. Mass Spectrom. 12, 1463-1474 (1998)
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 1463-1474
    • Campbell, J.M.1    Collings, B.A.2    Douglas, D.J.3
  • 33
    • 0342990831 scopus 로고
    • Planetary atmospheric simulation using molecular beams
    • French, J.B.: Planetary atmospheric simulation using molecular beams. CASI Trans. 3, 77-83 (1970)
    • (1970) CASI Trans. , vol.3 , pp. 77-83
    • French, J.B.1
  • 34
    • 37049077622 scopus 로고
    • Gas dynamics of the inductively coupled plasma mass spectrometry interface
    • 1:CAS:528:DyaL1cXmtFyktbw%3D 10.1039/ja9880300743
    • Douglas, D.J.; French, J.B.: Gas dynamics of the inductively coupled plasma mass spectrometry interface. J. Anal. At. Spectrom. 3, 743-747 (1988)
    • (1988) J. Anal. At. Spectrom. , vol.3 , pp. 743-747
    • Douglas, D.J.1    French, J.B.2
  • 35
    • 84891167880 scopus 로고
    • Background events in microchannel plates
    • 1:CAS:528:DyaL1cXks1aqsb4%3D 10.1109/23.12778
    • Siegmund, O.H.W.; Vallerga, J.; Wargelin, B.: Background events in microchannel plates. IEEE Trans. Nucl. Sci. 35, 524-528 (1988)
    • (1988) IEEE Trans. Nucl. Sci. , vol.35 , pp. 524-528
    • Siegmund, O.H.W.1    Vallerga, J.2    Wargelin, B.3
  • 36
    • 15944416777 scopus 로고    scopus 로고
    • A fast flow tube study of gas phase H/D exchange of multiply protonated ubiquitin
    • 1:CAS:528:DC%2BD2MXhsVyiu7o%3D 10.1021/jp044737c
    • Geller, O.; Lifshitz, C.: A fast flow tube study of gas phase H/D exchange of multiply protonated ubiquitin. J. Phys. Chem. A 109, 2217-2222 (2005)
    • (2005) J. Phys. Chem. A , vol.109 , pp. 2217-2222
    • Geller, O.1    Lifshitz, C.2
  • 37
    • 84864876729 scopus 로고    scopus 로고
    • How ubiquitin unfolds after transfer into the gas phase
    • 1:CAS:528:DC%2BC38Xms1WitLY%3D 10.1007/s13361-012-0370-6
    • Skinner, O.S.; McLafferty, F.W.; Breuker, K.: How ubiquitin unfolds after transfer into the gas phase. J. Am. Soc. Mass Spectrom. 23, 1011-1014 (2012)
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1011-1014
    • Skinner, O.S.1    McLafferty, F.W.2    Breuker, K.3
  • 38
    • 0141545030 scopus 로고    scopus 로고
    • Applying a new algorithm for obtaining site specific rate constants for H/D exchange of the gas phase proton-bound arginine dimer
    • 1:CAS:528:DC%2BD3sXnvVeksLg%3D 10.1016/j.cplett.2003.08.102
    • Reuben, B.G.; Ritov, Y.; Geller, O.; McFarland, M.A.; Marshall, A.G.; Lifshitz, C.: Applying a new algorithm for obtaining site specific rate constants for H/D exchange of the gas phase proton-bound arginine dimer. Chem. Phys. Lett. 380, 88-94 (2003)
    • (2003) Chem. Phys. Lett. , vol.380 , pp. 88-94
    • Reuben, B.G.1    Ritov, Y.2    Geller, O.3    McFarland, M.A.4    Marshall, A.G.5    Lifshitz, C.6
  • 40
    • 0020799447 scopus 로고
    • Multiple proton transfers within long-lived ion-molecule complexes
    • 1:CAS:528:DyaL3sXkslSisL8%3D 10.1021/ja00354a001
    • Squires, R.R.; Bierbaum, V.M.; Grabowski, J.J.; DePuy, C.H.: Multiple proton transfers within long-lived ion-molecule complexes. J. Am. Chem. Soc. 105, 5185-5192 (1983)
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5185-5192
    • Squires, R.R.1    Bierbaum, V.M.2    Grabowski, J.J.3    Depuy, C.H.4
  • 43
    • 33847797700 scopus 로고
    • Dynamics of proton transfer involving delocalized negative ions in the gas phase
    • 1:CAS:528:DyaE2sXkslKl 10.1021/ja00441a001
    • Farneth, W.E.; Brauman, J.I.: Dynamics of proton transfer involving delocalized negative ions in the gas phase. J. Am. Chem. Soc. 98, 7891-7898 (1976)
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 7891-7898
    • Farneth, W.E.1    Brauman, J.I.2
  • 44
    • 84902145795 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange in parallel with acid/base induced protein conformational change in electrospray droplets
    • 1:CAS:528:DC%2BC2cXpsValu7c%3D 10.1002/jms.3369
    • Kharlamova, A.; Fisher, C.M.; McLuckey, S.A.: Hydrogen/deuterium exchange in parallel with acid/base induced protein conformational change in electrospray droplets. J. Mass Spectrom. 49, 437-444 (2014)
    • (2014) J. Mass Spectrom. , vol.49 , pp. 437-444
    • Kharlamova, A.1    Fisher, C.M.2    McLuckey, S.A.3
  • 45
    • 84914751407 scopus 로고
    • Evaluated gas phase basicities and proton affinities of molecules; Heats of formation of protonated molecules
    • 1:CAS:528:DyaL2MXltFOksw%3D%3D 10.1063/1.555719
    • Lias, S.G.; Liebman, J.F.; Levin, R.D.: Evaluated gas phase basicities and proton affinities of molecules; heats of formation of protonated molecules. J. Phys. Chem. Ref. Data 13, 695-808 (1984)
    • (1984) J. Phys. Chem. Ref. Data , vol.13 , pp. 695-808
    • Lias, S.G.1    Liebman, J.F.2    Levin, R.D.3
  • 47
    • 0000149885 scopus 로고
    • Gas-phase proton transfer reactions involving multiply charged cytochrome c ions and water under thermal conditions
    • 1:CAS:528:DyaK3sXht1ShsrY%3D 10.1016/1044-0305(92)85003-3
    • Winger, B.E.; Light-Wahl, K.J.; Smith, R.D.: Gas-phase proton transfer reactions involving multiply charged cytochrome c ions and water under thermal conditions. J. Am. Soc. Mass Spectrom. 3, 624-630 (1992)
    • (1992) J. Am. Soc. Mass Spectrom. , vol.3 , pp. 624-630
    • Winger, B.E.1    Light-Wahl, K.J.2    Smith, R.D.3
  • 48
    • 0020490571 scopus 로고
    • The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications
    • 1:CAS:528:DyaL38XitFakt78%3D
    • Koppenol, W.H.; Margoliash, E.: The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications. J. Biol. Chem. 257, 4426-4437 (1982)
    • (1982) J. Biol. Chem. , vol.257 , pp. 4426-4437
    • Koppenol, W.H.1    Margoliash, E.2
  • 50
    • 0025088690 scopus 로고
    • Horse heart ferri-cytochrome c: Conformation and heme configuration of low ionic strength acidic forms
    • Meyer, Y.P.; Saturno, A.F.: Horse heart ferri-cytochrome c: conformation and heme configuration of low ionic strength acidic forms. J. Protein Chem. 9, 379-387 (1990)
    • (1990) J. Protein Chem. , vol.9 , pp. 379-387
    • Meyer, Y.P.1    Saturno, A.F.2
  • 51
    • 0030939178 scopus 로고    scopus 로고
    • Protein structure in vacuo: Gas-phase conformations of BPTI and cytochrome c
    • 1:CAS:528:DyaK2sXit1Kntb4%3D 10.1021/ja9619059
    • Shelimov, K.B.; Clemmer, D.E.; Hudgins, R.R.; Jarrold, M.F.: Protein structure in vacuo: gas-phase conformations of BPTI and cytochrome c. J. Am. Chem. Soc. 119, 2240-2248 (1997)
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2240-2248
    • Shelimov, K.B.1    Clemmer, D.E.2    Hudgins, R.R.3    Jarrold, M.F.4
  • 52
    • 0029987289 scopus 로고    scopus 로고
    • "denaturation" and refolding of cytochrome c in vacuo
    • 1:CAS:528:DyaK28XmtFKkt7o%3D 10.1021/ja962419o
    • Shelimov, K.B.; Jarrold, M.F.: "Denaturation" and refolding of cytochrome c in vacuo. J. Am. Chem. Soc. 118, 10313-10314 (1996)
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10313-10314
    • Shelimov, K.B.1    Jarrold, M.F.2
  • 54
    • 0002426844 scopus 로고
    • Observation and implications of high mass-to-charge ratio ions from electrospray ionization mass spectrometry
    • 1:CAS:528:DyaK2cXivFehurg%3D 10.1016/1044-0305(93)85015-P
    • Winger, B.E.; Light-Wahl, K.J.; Ogorzalek Loo, R.R.; Udseth, H.R.; Smith, R.D.: Observation and implications of high mass-to-charge ratio ions from electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 4, 536-545 (1993)
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 536-545
    • Winger, B.E.1    Light-Wahl, K.J.2    Ogorzalek Loo, R.R.3    Udseth, H.R.4    Smith, R.D.5
  • 55
    • 0001686153 scopus 로고
    • Collision cross sections for protein ions
    • 1:CAS:528:DyaK2cXht1yqtbw%3D 10.1016/1044-0305(93)85025-S
    • Covey, T.; Douglas, D.J.: Collision cross sections for protein ions. J. Am. Soc. Mass Spectrom. 4, 616-623 (1993)
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 616-623
    • Covey, T.1    Douglas, D.J.2
  • 56
    • 0032550657 scopus 로고    scopus 로고
    • Gaseous conformational structures of cytochrome c
    • 1:CAS:528:DyaK1cXis12qs7w%3D 10.1021/ja9728076
    • McLafferty, F.W.; Guan, Z.; Haupts, U.; Wood, T.D.; Kelleher, N.L.: Gaseous conformational structures of cytochrome c. J. Am. Chem. Soc. 120, 4732-4740 (1998)
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4732-4740
    • McLafferty, F.W.1    Guan, Z.2    Haupts, U.3    Wood, T.D.4    Kelleher, N.L.5
  • 57
    • 18744397503 scopus 로고    scopus 로고
    • Secondary and tertiary structures of gaseous protein ions characterized by ECD mass spectrometry and photofragment spectroscopy
    • 1:CAS:528:DC%2BD38Xps1egtb0%3D 10.1073/pnas.212643599
    • Oh, H.; Breuker, K.; Sze, S.K.; Ge, Y.; Carpenter, B.K.; McLafferty, F.W.: Secondary and tertiary structures of gaseous protein ions characterized by ECD mass spectrometry and photofragment spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 99, 15863-15868 (2002)
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 15863-15868
    • Oh, H.1    Breuker, K.2    Sze, S.K.3    Ge, Y.4    Carpenter, B.K.5    McLafferty, F.W.6
  • 58
    • 34547993848 scopus 로고    scopus 로고
    • The dynamics of water evaporation from partially solvated cytochrome c in the gas phase
    • 1:CAS:528:DC%2BD2sXptVWqsbs%3D 10.1039/b705905a
    • Steinberg, M.Z.; Breuker, K.; Elber, R.; Gerber, R.B.: The dynamics of water evaporation from partially solvated cytochrome c in the gas phase. Phys. Chem. Chem. Phys. 9, 4690-4697 (2007)
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 4690-4697
    • Steinberg, M.Z.1    Breuker, K.2    Elber, R.3    Gerber, R.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.