메뉴 건너뛰기




Volumn 65, Issue , 2014, Pages 175-196

Ion mobility analysis of molecular dynamics

Author keywords

biomolecule; conformation; gas phase structure; IMS IMS; solution structure

Indexed keywords

CONFORMATIONS; ION MOBILITY SPECTROMETERS; IONS; MASS SPECTROMETRY; PEPTIDES; PHASE STRUCTURE;

EID: 84897544108     PISSN: 0066426X     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev-physchem-040513-103644     Document Type: Article
Times cited : (167)

References (88)
  • 1
    • 77955876447 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics in cell biology
    • Walther TC, Mann M. 2010. Mass spectrometry-based proteomics in cell biology. J. Cell Biol. 190:491-500
    • (2010) J. Cell Biol , vol.190 , pp. 491-500
    • Walther, T.C.1    Mann, M.2
  • 2
    • 0041317054 scopus 로고    scopus 로고
    • Electrospray wings for molecular elephants (Nobel lecture
    • Fenn JB. 2003. Electrospray wings for molecular elephants (Nobel lecture). Angew. Chem. Int. Ed. Engl. 42:3871-94
    • (2003) Angew. Chem. Int. Ed. Engl , vol.42 , pp. 3871-3894
    • Fenn, J.B.1
  • 3
    • 0030905633 scopus 로고    scopus 로고
    • Ion mobility measurements and their applications to clusters and biomolecules
    • Clemmer DE, Jarrold MF. 1997. Ion mobility measurements and their applications to clusters and biomolecules. J. Mass Spectrom. 32:577-92
    • (1997) J. Mass Spectrom , vol.32 , pp. 577-592
    • Clemmer, D.E.1    Jarrold, M.F.2
  • 4
    • 1642290025 scopus 로고    scopus 로고
    • Gas-phase conformations: The ion mobility/ion chromatography method
    • Wyttenbach T, Bowers MT. 2003. Gas-phase conformations: The ion mobility/ion chromatography method. Top. Curr. Chem. 225:207-32
    • (2003) Top. Curr. Chem , vol.225 , pp. 207-232
    • Wyttenbach, T.1    Bowers, M.T.2
  • 5
  • 6
    • 82555179707 scopus 로고    scopus 로고
    • Developments in ionmobility: Theory, instrumentation, and applications
    • ed. CL Wilkins, S Trimpin. Boca Raton, FL: CRC
    • Wyttenbach T, Gidden J, BowersMT. 2011. Developments in ionmobility: Theory, instrumentation, and applications. In Ion Mobility Spectrometry-Mass Spectrometry, ed. CL Wilkins, S Trimpin, pp. 3-30. Boca Raton, FL: CRC
    • (2011) Ion Mobility Spectrometry-Mass Spectrometry , pp. 3-30
    • Wyttenbach, T.1    Gidden, J.2    Bowers, M.T.3
  • 9
    • 84874025375 scopus 로고    scopus 로고
    • Factors contributing to the collision cross section of polyatomic ions in the kilodalton to gigadalton range: Application to ion mobility measurements
    • Wyttenbach T, Bleiholder C, Bowers MT. 2013. Factors contributing to the collision cross section of polyatomic ions in the kilodalton to gigadalton range: Application to ion mobility measurements. Anal. Chem. 85:2191-99
    • (2013) Anal. Chem , vol.85 , pp. 2191-2199
    • Wyttenbach, T.1    Bleiholder, C.2    Bowers, M.T.3
  • 10
    • 0034819873 scopus 로고    scopus 로고
    • Gas-phase conformations and folding energetics of oligonucleotides: DTG-And dGT-P
    • Gidden J, Bushnell JE, Bowers MT. 2001. Gas-phase conformations and folding energetics of oligonucleotides: DTG-And dGT-P. J. Am. Chem. Soc. 123:5610-11
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 5610-5611
    • Gidden, J.1    Bushnell, J.E.2    Bowers, M.T.3
  • 11
    • 0036769485 scopus 로고    scopus 로고
    • Gas-phase conformational and energetic properties of deprotonated dinucleotides
    • Gidden J, Bowers MT. 2002. Gas-phase conformational and energetic properties of deprotonated dinucleotides. Eur. Phys. J. D 20:409-19
    • (2002) Eur. Phys. J. , vol.D20 , pp. 409-419
    • Gidden, J.1    Bowers, M.T.2
  • 12
    • 84875463071 scopus 로고
    • Matrix-Assisted laser desorption/ionization mass spectrometry of biopolymers
    • Hillenkamp F, Karas M, Beavis RC, Chait BT. 1991. Matrix-Assisted laser desorption/ionization mass spectrometry of biopolymers. Anal. Chem. 63:A1193-202
    • (1991) Anal. Chem , vol.63
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 13
    • 0042318496 scopus 로고    scopus 로고
    • The origin of macromolecule ionization by laser irradiation (Nobel lecture
    • Tanaka K. 2003. The origin of macromolecule ionization by laser irradiation (Nobel lecture). Angew. Chem. Int. Ed. Engl. 42:3860-70
    • (2003) Angew. Chem. Int. Ed. Engl , vol.42 , pp. 3860-3870
    • Tanaka, K.1
  • 15
    • 0000910245 scopus 로고
    • Analysis for ion drift tube experiments
    • ed. EWMcDaniel, MRC McDowell. Amsterdam North-Holland
    • Gatland IR. 1974. Analysis for ion drift tube experiments. In Case Studies in Atomic Collision Physics, Vol. 4, ed. EWMcDaniel, MRC McDowell, pp. 369-437. Amsterdam: North-Holland
    • (1974) Case Studies in Atomic Collision Physics , vol.4 , pp. 369-437
    • Gatland, I.R.1
  • 17
    • 33645831109 scopus 로고
    • The kinetics of the recombination of methyl radicals and iodine atoms
    • Marcus RA, Rice OK. 1951. The kinetics of the recombination of methyl radicals and iodine atoms. J. Phys. Colloid Chem. 55:894-908
    • (1951) J. Phys. Colloid Chem , vol.55 , pp. 894-908
    • Marcus, R.A.1    Rice, O.K.2
  • 18
    • 0025390935 scopus 로고
    • Mopac: A semiempirical molecular orbital program
    • Stewart JJ. 1990. MOPAC: A semiempirical molecular orbital program. J. Comput. Aided Mol. Des. 4:1-105
    • (1990) J. Comput. Aided Mol. Des , vol.4 , pp. 1-105
    • Stewart, J.J.1
  • 20
    • 0029134442 scopus 로고
    • Conformation of macromolecules in the gas phase: Use of matrix-Assisted laser-desorption methods in ion chromatography
    • von Helden G, Wyttenbach T, Bowers MT. 1995. Conformation of macromolecules in the gas phase: Use of matrix-Assisted laser-desorption methods in ion chromatography. Science 267:1483-85
    • (1995) Science , vol.267 , pp. 1483-1485
    • Von Helden, G.1    Wyttenbach, T.2    Bowers, M.T.3
  • 21
    • 0002677181 scopus 로고    scopus 로고
    • Conformations of alkali ion cationized polyethers in the gas phase: Polyethylene glycol and bis[(benzo-15-crown 5)-15-ylmethyl] pimelate
    • Wyttenbach T, vonHeldenG, BowersMT. 1997. Conformations of alkali ion cationized polyethers in the gas phase: Polyethylene glycol and bis[(benzo-15-crown-5)-15-ylmethyl] pimelate. Int. J. Mass Spectrom. 165:377-90
    • (1997) Int. J. Mass Spectrom , vol.165 , pp. 377-390
    • Wyttenbach, T.1    Von Helden, G.2    Bowers, M.T.3
  • 22
    • 0001720683 scopus 로고
    • Inclusion of aMALDI ion source in the ion chromatography technique: Conformational information on polymer and biomolecular ions
    • vonHeldenG, Wyttenbach T, Bowers MT. 1995. Inclusion of aMALDI ion source in the ion chromatography technique: Conformational information on polymer and biomolecular ions. Int. J. Mass Spectrom. Ion Process. 146:349-64
    • (1995) Int. J. Mass Spectrom. Ion Process , vol.146 , pp. 349-364
    • Von Helden, G.1    Wyttenbach, T.2    Bowers, M.T.3
  • 23
    • 0034679010 scopus 로고    scopus 로고
    • Gas-phase conformations of synthetic polymers: Poly(ethylene glycol), poly(propylene glycol), and poly(tetramethylene glycol
    • Gidden J, Wyttenbach T, Jackson AT, Scrivens JH, Bowers MT. 2000. Gas-phase conformations of synthetic polymers: Poly(ethylene glycol), poly(propylene glycol), and poly(tetramethylene glycol). J. Am. Chem. Soc. 122:4692-99
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 4692-4699
    • Gidden, J.1    Wyttenbach, T.2    Jackson, A.T.3    Scrivens, J.H.4    Bowers, M.T.5
  • 24
    • 0033654137 scopus 로고    scopus 로고
    • Peptides and proteins in the vapor phase
    • Jarrold MF. 2000. Peptides and proteins in the vapor phase. Annu. Rev. Phys. Chem. 51:179-207
    • (2000) Annu. Rev. Phys. Chem , vol.51 , pp. 179-207
    • Jarrold, M.F.1
  • 26
    • 34047144959 scopus 로고    scopus 로고
    • Helices and sheets in vacuo
    • Jarrold MF. 2007. Helices and sheets in vacuo. Phys. Chem. Chem. Phys. 9:1659-71
    • (2007) Phys. Chem. Chem. Phys , vol.9 , pp. 1659-1671
    • Jarrold, M.F.1
  • 27
    • 0034695349 scopus 로고    scopus 로고
    • Conformations of biopolymers in the gas phase: A new mass spectrometric method
    • Gill AC, Jennings KR, Wyttenbach T, Bowers MT. 2000. Conformations of biopolymers in the gas phase: A new mass spectrometric method. Int. J. Mass Spectrom. 196:685-97
    • (2000) Int. J. Mass Spectrom , vol.196 , pp. 685-697
    • Gill, A.C.1    Jennings, K.R.2    Wyttenbach, T.3    Bowers, M.T.4
  • 28
    • 75649087404 scopus 로고    scopus 로고
    • Factors that influence helical preferences for singly charged gas-phase peptide ions: The effects of multiple potential charge-carrying sites
    • McLean JR, McLean JA, WuZ, Becker C, Ṕerez LM, et al. 2010. Factors that influence helical preferences for singly charged gas-phase peptide ions: The effects of multiple potential charge-carrying sites. J. Phys. Chem. B 114:809-16
    • (2010) J. Phys. Chem , vol.B114 , pp. 809-816
    • McLean, J.R.1    McLean, J.A.2    Wu, Z.3    Becker, C.4    Ṕerez, L.M.5
  • 29
    • 0000924229 scopus 로고    scopus 로고
    • Conformations of unsolvated glycine-based peptides
    • Hudgins RR, Jarrold MF. 2000. Conformations of unsolvated glycine-based peptides. J. Phys. Chem. B 104:2154-58
    • (2000) J. Phys. Chem , vol.B104 , pp. 2154-2158
    • Hudgins, R.R.1    Jarrold, M.F.2
  • 31
    • 0032572063 scopus 로고    scopus 로고
    • Salt bridge structures in the absence of solvent? The case for the oligoglycines
    • Wyttenbach T, Bushnell JE, BowersMT. 1998. Salt bridge structures in the absence of solvent? The case for the oligoglycines. J. Am. Chem. Soc. 120:5098-103
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 5098-5103
    • Wyttenbach, T.1    Bushnell, J.E.2    Bowers, M.T.3
  • 32
    • 0033014467 scopus 로고    scopus 로고
    • Conformations of GlynH+ and AlanH+ peptides in the gas phase
    • Hudgins RR, Mao Y, RatnerMA, Jarrold MF. 1999. Conformations of GlynH+ and AlanH+ peptides in the gas phase. Biophys. J. 76:1591-97
    • (1999) Biophys. J. , vol.76 , pp. 1591-1597
    • Hudgins, R.R.1    Mao, Y.2    Ratner, M.A.3    Jarrold, M.F.4
  • 33
    • 0001070559 scopus 로고    scopus 로고
    • Intrinsic size parameters for Val, Ile, Leu, Gln, Thr, Phe, and Trp residues from ion mobility measurements of polyamino acid ions
    • Henderson SC, Li JW, Counterman AE, Clemmer DE. 1999. Intrinsic size parameters for Val, Ile, Leu, Gln, Thr, Phe, and Trp residues from ion mobility measurements of polyamino acid ions. J. Phys. Chem. B 103:8780-85
    • (1999) J. Phys. Chem , vol.B103 , pp. 8780-8785
    • Henderson, S.C.1    Li, J.W.2    Counterman, A.E.3    Clemmer, D.E.4
  • 34
    • 20444495558 scopus 로고    scopus 로고
    • Evaluation of ion mobility spectroscopy for determining charge-solvated versus salt-bridge structures of protonated trimers
    • Wong RL, Williams ER, Counterman AE, Clemmer DE. 2005. Evaluation of ion mobility spectroscopy for determining charge-solvated versus salt-bridge structures of protonated trimers. J. Am. Soc. Mass Spectrom. 16:1009-19
    • (2005) J. Am. Soc. Mass Spectrom , vol.16 , pp. 1009-1019
    • Wong, R.L.1    Williams, E.R.2    Counterman, A.E.3    Clemmer, D.E.4
  • 35
    • 84931128415 scopus 로고
    • Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin
    • Rocha e Silva M, Beraldo WT, Rosenfeld G. 1949. Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin. Am. J. Physiol. 156:261-73
    • (1949) Am. J. Physiol , vol.156 , pp. 261-273
    • Rocha, E.1    Silva, M.2    Beraldo, W.T.3    Rosenfeld, G.4
  • 37
    • 0029841917 scopus 로고    scopus 로고
    • Gas-phase conformation of biological molecules: Bradykinin
    • Wyttenbach T, von Helden G, Bowers MT. 1996. Gas-phase conformation of biological molecules: Bradykinin. J. Am. Chem. Soc. 118:8355-64
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 8355-8364
    • Wyttenbach, T.1    Von Helden, G.2    Bowers, M.T.3
  • 38
    • 0029768104 scopus 로고    scopus 로고
    • Blackbody infrared radiative dissociation of bradykinin and its analogues: Energetics, dynamics, and evidence for salt-bridge structures in the gas phase
    • Schnier PD, Price WD, Jockusch RA, Williams ER. 1996. Blackbody infrared radiative dissociation of bradykinin and its analogues: Energetics, dynamics, and evidence for salt-bridge structures in the gas phase. J. Am. Chem. Soc. 118:7178-89
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 7178-7189
    • Schnier, P.D.1    Price, W.D.2    Jockusch, R.A.3    Williams, E.R.4
  • 39
    • 0000271162 scopus 로고    scopus 로고
    • Rate and extent of gas phase hydrogen/deuterium exchange of bradykinins: Evidence for peptide zwitterions in the gas phase
    • Freitas MA, Marshall AG. 1999. Rate and extent of gas phase hydrogen/deuterium exchange of bradykinins: Evidence for peptide zwitterions in the gas phase. Int. J. Mass Spectrom. 182-183:221-31
    • (1999) Int. J. Mass Spectrom , vol.182 , pp. 221-231
    • Freitas, M.A.1    Marshall, A.G.2
  • 40
    • 33646270190 scopus 로고    scopus 로고
    • Gaseous bradykinin and its singly, doubly, and triply protonated forms: A first-principles study
    • Rodriguez CF, Orlova G, Guo Y, Li X, Siu C-K, et al. 2006. Gaseous bradykinin and its singly, doubly, and triply protonated forms: A first-principles study. J. Phys. Chem. B 110:7528-37
    • (2006) J. Phys. Chem , vol.B110 , pp. 7528-7537
    • Rodriguez, C.F.1    Orlova, G.2    Guo, Y.3    Li, X.4    Siu, C.-K.5
  • 41
    • 0033556190 scopus 로고    scopus 로고
    • ESI/ion trap/ion mobility/time-offlightmass spectrometry for rapid and sensitive analysis of biomolecular mixtures
    • Henderson SC, Valentine SJ, Counterman AE, Clemmer DE. 1999. ESI/ion trap/ion mobility/time-offlightmass spectrometry for rapid and sensitive analysis of biomolecular mixtures. Anal. Chem. 71:291-301
    • (1999) Anal. Chem , vol.71 , pp. 291-301
    • Henderson, S.C.1    Valentine, S.J.2    Counterman, A.E.3    Clemmer, D.E.4
  • 42
    • 77953469651 scopus 로고    scopus 로고
    • Evidence for a quasi-equilibrium distribution of states for bradykinin [M + 3H]3+ ions in the gas phase
    • Pierson NA, Valentine SJ, Clemmer DE. 2010. Evidence for a quasi-equilibrium distribution of states for bradykinin [M + 3H]3+ ions in the gas phase. J. Phys. Chem. B 114:7777-83
    • (2010) J. Phys. Chem , vol.B114 , pp. 7777-7783
    • Pierson, N.A.1    Valentine, S.J.2    Clemmer, D.E.3
  • 43
    • 80052326593 scopus 로고    scopus 로고
    • Number of solution states of bradykinin from ion mobility and mass spectrometry measurements
    • Pierson NA, Chen L, Valentine SJ, Russell DH, Clemmer DE. 2011. Number of solution states of bradykinin from ion mobility and mass spectrometry measurements. J. Am. Chem. Soc. 133:13810-13
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 13810-13813
    • Pierson, N.A.1    Chen, L.2    Valentine, S.J.3    Russell, D.H.4    Clemmer, D.E.5
  • 44
    • 41049090800 scopus 로고    scopus 로고
    • The structure of the neuropeptide bradykinin bound to the human G-protein coupled receptor bradykinin B2 as determined by solid-state NMR spectroscopy
    • Lopez JJ, Shukla AK, Reinhart C, Schwalbe H, Michel H, Glaubitz C. 2008. The structure of the neuropeptide bradykinin bound to the human G-protein coupled receptor bradykinin B2 as determined by solid-state NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 47:1668-71
    • (2008) Angew. Chem. Int. Ed. Engl , vol.47 , pp. 1668-1671
    • Lopez, J.J.1    Shukla, A.K.2    Reinhart, C.3    Schwalbe, H.4    Michel, H.5    Glaubitz, C.6
  • 46
    • 0028439188 scopus 로고
    • NMR and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9:1 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles
    • Young JK, Hicks RP. 1994. NMR and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9:1 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles. Biopolymers 34:611-23
    • (1994) Biopolymers , vol.34 , pp. 611-623
    • Young, J.K.1    Hicks, R.P.2
  • 47
    • 0035050370 scopus 로고    scopus 로고
    • Recent advances in NMR: Expanding its role in rational drug design
    • Hicks RP. 2001. Recent advances in NMR: Expanding its role in rational drug design. Curr. Med. Chem. 8:627-50
    • (2001) Curr. Med. Chem , vol.8 , pp. 627-650
    • Hicks, R.P.1
  • 48
    • 1342301591 scopus 로고    scopus 로고
    • Conformational alteration of bradykinin in presence of GM1 micelle
    • Chatterjee C, Mukhopadhyay C. 2004. Conformational alteration of bradykinin in presence of GM1 micelle. Biochem. Biophys. Res. Commun. 315:866-71
    • (2004) Biochem. Biophys. Res. Commun , vol.315 , pp. 866-871
    • Chatterjee, C.1    Mukhopadhyay, C.2
  • 50
    • 84874625189 scopus 로고    scopus 로고
    • Cis-Trans isomerizations of proline residues are key to bradykinin conformations
    • Pierson NA, Chen L, Russell DH, Clemmer DE. 2013. Cis-Trans isomerizations of proline residues are key to bradykinin conformations. J. Am. Chem. Soc. 135:3186-92
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 3186-3192
    • Pierson, N.A.1    Chen, L.2    Russell, D.H.3    Clemmer, D.E.4
  • 51
    • 0028928486 scopus 로고
    • Biomolecular folding in vacuo!!!(?
    • Wolynes PG. 1995. Biomolecular folding in vacuo!!!(?). Proc. Natl. Acad. Sci. USA 92:2426-27
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2426-2427
    • Wolynes, P.G.1
  • 52
  • 53
    • 80054892557 scopus 로고    scopus 로고
    • Structural stability from solution to the gas phase: Native solution structure of ubiquitin survives analysis in a solvent-free ion mobility-mass spectrometry environment
    • Wyttenbach T, Bowers MT. 2011. Structural stability from solution to the gas phase: Native solution structure of ubiquitin survives analysis in a solvent-free ion mobility-mass spectrometry environment. J. Phys. Chem. B 115:12266-75
    • (2011) J. Phys. Chem , vol.B115 , pp. 12266-12275
    • Wyttenbach, T.1    Bowers, M.T.2
  • 54
    • 79960007398 scopus 로고    scopus 로고
    • What happens to hydrophobic interactions during transfer from the solution to the gas phase? The case of electrospray-based soft ionization methods
    • Barylyuk K, BalabinRM, Gr ünsteinD, Kikkeri R, Frankevich V, et al. 2011. What happens to hydrophobic interactions during transfer from the solution to the gas phase? The case of electrospray-based soft ionization methods. J. Am. Soc. Mass Spectrom. 22:1167-77
    • (2011) J. Am. Soc. Mass Spectrom , vol.22 , pp. 1167-1177
    • Barylyuk, K.1    Balabin, R.M.2    Grünstein, D.3    Kikkeri, R.4    Frankevich, V.5
  • 55
    • 33748572634 scopus 로고    scopus 로고
    • Aspects of native proteins are retained in vacuum
    • Ruotolo BT, Robinson CV. 2006. Aspects of native proteins are retained in vacuum. Curr. Opin. Chem. Biol. 10:402-8
    • (2006) Curr. Opin. Chem. Biol , vol.10 , pp. 402-408
    • Ruotolo, B.T.1    Robinson, C.V.2
  • 56
    • 79959456892 scopus 로고    scopus 로고
    • Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes
    • Barrera NP, Robinson CV. 2011. Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes. Annu. Rev. Biochem. 80:247-71
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 247-271
    • Barrera, N.P.1    Robinson, C.V.2
  • 57
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 ̊A resolution
    • Vijay-Kumar S, Bugg CE, Cook WJ. 1987. Structure of ubiquitin refined at 1.8 ̊A resolution. J. Mol. Biol. 194:531-44
    • (1987) J. Mol. Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 58
    • 0342813119 scopus 로고    scopus 로고
    • Backbone dynamics and structural characterization of the partially folded A state of ubiquitin by 1H, 13C, and 15N nuclear magnetic resonance spectroscopy
    • Brutscher B, Bruschweiler R, Ernst RR. 1997. Backbone dynamics and structural characterization of the partially folded A state of ubiquitin by 1H, 13C, and 15N nuclear magnetic resonance spectroscopy. Biochemistry 36:13043-53
    • (1997) Biochemistry , vol.36 , pp. 13043-13053
    • Brutscher, B.1    Bruschweiler, R.2    Ernst, R.R.3
  • 59
    • 0025674590 scopus 로고
    • Probing conformational changes in proteins by mass spectrometry
    • Chowdhury SK, Katta V, Chait BT. 1990. Probing conformational changes in proteins by mass spectrometry. J. Am. Chem. Soc. 112:9012-13
    • (1990) J. Am. Chem. Soc , vol.112 , pp. 9012-9013
    • Chowdhury, S.K.1    Katta, V.2    Chait, B.T.3
  • 60
    • 0026134908 scopus 로고
    • Conformational changes in proteins probed by hydrogen-exchange electrosprayionization mass spectrometry
    • Katta V, Chait BT. 1991. Conformational changes in proteins probed by hydrogen-exchange electrosprayionization mass spectrometry. Rapid Commun. Mass Spectrom. 5:214-17
    • (1991) Rapid Commun. Mass Spectrom , vol.5 , pp. 214-217
    • Katta, V.1    Chait, B.T.2
  • 61
    • 0032232233 scopus 로고    scopus 로고
    • Unfolding of proteins monitored by electrospray ionization mass spectrometry: A comparison of positive and negative ion modes
    • Konermann L, Douglas DJ. 1998. Unfolding of proteins monitored by electrospray ionization mass spectrometry: A comparison of positive and negative ion modes. J. Am. Soc. Mass Spectrom. 9:1248-54
    • (1998) J. Am. Soc. Mass Spectrom , vol.9 , pp. 1248-1254
    • Konermann, L.1    Douglas, D.J.2
  • 62
    • 0028855096 scopus 로고
    • Naked protein conformations: Cytochrome c in the gas phase
    • Clemmer DE, Hudgins RR, Jarrold MF. 1995. Naked protein conformations: Cytochrome c in the gas phase. J. Am. Chem. Soc. 117:10141-42
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 10141-10142
    • Clemmer, D.E.1    Hudgins, R.R.2    Jarrold, M.F.3
  • 63
    • 0001604844 scopus 로고    scopus 로고
    • Disulfide-intact and-reduced lysozyme in the gas phase: Conformations and pathways of folding and unfolding
    • Valentine SJ, Anderson JG, Ellington AD, Clemmer DE. 1997. Disulfide-intact and-reduced lysozyme in the gas phase: Conformations and pathways of folding and unfolding. J. Phys. Chem. B 101:3891-900
    • (1997) J. Phys. Chem , vol.B101 , pp. 3891-3900
    • Valentine, S.J.1    Anderson, J.G.2    Ellington, A.D.3    Clemmer, D.E.4
  • 64
    • 0030913630 scopus 로고    scopus 로고
    • Conformations, unfolding, and refolding of apomyoglobin in vacuum: An activation barrier for gas-phase protein folding
    • Shelimov KB, Jarrold MF. 1997. Conformations, unfolding, and refolding of apomyoglobin in vacuum: An activation barrier for gas-phase protein folding. J. Am. Chem. Soc. 119:2987-94
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 2987-2994
    • Shelimov, K.B.1    Jarrold, M.F.2
  • 65
    • 0345600790 scopus 로고    scopus 로고
    • A capillary mixer with adjustable reaction chamber volume for millisecond time-resolved studies by electrospray mass spectrometry
    • Wilson DJ, Konermann L. 2003. A capillary mixer with adjustable reaction chamber volume for millisecond time-resolved studies by electrospray mass spectrometry. Anal. Chem. 75:6408-14
    • (2003) Anal. Chem , vol.75 , pp. 6408-6414
    • Wilson, D.J.1    Konermann, L.2
  • 67
    • 0037168359 scopus 로고    scopus 로고
    • Structural transitions of electrosprayed ubiquitin ions stored in an ion trap over ∼10 ms to 30 s
    • Myung S, Badman ER, Lee YJ, Clemmer DE. 2002. Structural transitions of electrosprayed ubiquitin ions stored in an ion trap over ∼10 ms to 30 s. J. Phys. Chem. A 106:9976-82
    • (2002) J. Phys. Chem , vol.A106 , pp. 9976-9982
    • Myung, S.1    Badman, E.R.2    Lee, Y.J.3    Clemmer, D.E.4
  • 68
    • 0030580028 scopus 로고    scopus 로고
    • An exact hard-spheres scattering model for themobilities of polyatomic ions
    • Shvartsburg AA, Jarrold MF. 1996. An exact hard-spheres scattering model for themobilities of polyatomic ions. Chem. Phys. Lett. 261:86-91
    • (1996) Chem. Phys. Lett , vol.261 , pp. 86-91
    • Shvartsburg, A.A.1    Jarrold, M.F.2
  • 70
    • 33646357505 scopus 로고    scopus 로고
    • Evidence for many resolvable structures within conformation types of electrosprayed ubiquitin ions
    • Koeniger SL, Merenbloom SI, Clemmer DE. 2006. Evidence for many resolvable structures within conformation types of electrosprayed ubiquitin ions. J. Phys. Chem. B 110:7017-21
    • (2006) J. Phys. Chem , vol.B110 , pp. 7017-7021
    • Koeniger, S.L.1    Merenbloom, S.I.2    Clemmer, D.E.3
  • 71
    • 33748338997 scopus 로고    scopus 로고
    • Transfer of structural elements from compact to extended states in unsolvated ubiquitin
    • Koeniger SL, Merenbloom SI, Sevugarajan S, Clemmer DE. 2006. Transfer of structural elements from compact to extended states in unsolvated ubiquitin. J. Am. Chem. Soc. 128:11713-19
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 11713-11719
    • Koeniger, S.L.1    Merenbloom, S.I.2    Sevugarajan, S.3    Clemmer, D.E.4
  • 72
    • 84858327195 scopus 로고    scopus 로고
    • Conformation types of ubiquitin [M+8H]8+ ions from water:methanol solutions: Evidence for the N and A states in aqueous solution
    • Shi H, Pierson NA, Valentine SJ, Clemmer DE. 2012. Conformation types of ubiquitin [M+8H]8+ ions from water:methanol solutions: Evidence for the N and A states in aqueous solution. J. Phys. Chem. B 116:3344-52
    • (2012) J. Phys. Chem , vol.B116 , pp. 3344-3352
    • Shi, H.1    Pierson, N.A.2    Valentine, S.J.3    Clemmer, D.E.4
  • 73
    • 46749146468 scopus 로고    scopus 로고
    • Conformational evolution of ubiquitin ions in electrospray mass spectrometry: Molecular dynamics simulations at gradually increasing temperatures
    • Segev E, Wyttenbach T, Bowers MT, Gerber RB. 2008. Conformational evolution of ubiquitin ions in electrospray mass spectrometry: Molecular dynamics simulations at gradually increasing temperatures. Phys. Chem. Chem. Phys. 10:3077-82
    • (2008) Phys. Chem. Chem. Phys , vol.10 , pp. 3077-3082
    • Segev, E.1    Wyttenbach, T.2    Bowers, M.T.3    Gerber, R.B.4
  • 74
    • 33846444321 scopus 로고    scopus 로고
    • Resolution and structural transitions of elongated states of ubiquitin
    • Koeniger SL, Clemmer DE. 2007. Resolution and structural transitions of elongated states of ubiquitin. J. Am. Soc. Mass Spectrom. 18:322-31
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 322-331
    • Koeniger, S.L.1    Clemmer, D.E.2
  • 75
    • 79952980494 scopus 로고    scopus 로고
    • Protein-nucleic acid complexes and the role of mass spectrometry in their structure determination
    • Park AY, Robinson CV. 2011. Protein-nucleic acid complexes and the role of mass spectrometry in their structure determination. Crit. Rev. Biochem. Mol. 46:152-64
    • (2011) Crit. Rev. Biochem. Mol , vol.46 , pp. 152-164
    • Park, A.Y.1    Robinson, C.V.2
  • 76
    • 84862663706 scopus 로고    scopus 로고
    • Integrating mass spectrometry of intact protein complexes into structural proteomics
    • Hyung SJ, Ruotolo BT. 2012. Integrating mass spectrometry of intact protein complexes into structural proteomics. Proteomics 12:1547-64
    • (2012) Proteomics , vol.12 , pp. 1547-1564
    • Hyung, S.J.1    Ruotolo, B.T.2
  • 78
    • 34249947523 scopus 로고    scopus 로고
    • Intermolecular interactions in biomolecular systems examined by mass spectrometry
    • Wyttenbach T, Bowers MT. 2007. Intermolecular interactions in biomolecular systems examined by mass spectrometry. Annu. Rev. Phys. Chem. 58:511-33
    • (2007) Annu. Rev. Phys. Chem , vol.58 , pp. 511-533
    • Wyttenbach, T.1    Bowers, M.T.2
  • 79
    • 33749832945 scopus 로고    scopus 로고
    • Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach
    • Teplow DB, Lazo ND, Bitan G, Bernstein S, Wyttenbach T, et al. 2006. Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach. Acc. Chem. Res. 39:635-45
    • (2006) Acc. Chem. Res , vol.39 , pp. 635-645
    • Teplow, D.B.1    Lazo, N.D.2    Bitan, G.3    Bernstein, S.4    Wyttenbach, T.5
  • 80
    • 67849106670 scopus 로고    scopus 로고
    • Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
    • Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, et al. 2009. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 1:326-31
    • (2009) Nat. Chem , vol.1 , pp. 326-331
    • Bernstein, S.L.1    Dupuis, N.F.2    Lazo, N.D.3    Wyttenbach, T.4    Condron, M.M.5
  • 81
    • 79251631002 scopus 로고    scopus 로고
    • Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation
    • Bleiholder C, Dupuis NF, Wyttenbach T, Bowers MT. 2011. Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation. Nat. Chem. 3:172-77
    • (2011) Nat. Chem , vol.3 , pp. 172-177
    • Bleiholder, C.1    Dupuis, N.F.2    Wyttenbach, T.3    Bowers, M.T.4
  • 82
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • Kirkitadze MD, Bitan G, Teplow DB. 2002. Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies. J. Neurosci. Res. 69:567-77
    • (2002) J. Neurosci. Res , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 83
    • 0029671001 scopus 로고    scopus 로고
    • Structural studies of opioid peptides: A review of recent progress in X-ray diffraction studies
    • Deschamps JR, George C, Flippen-Anderson JL. 1996. Structural studies of opioid peptides: A review of recent progress in X-ray diffraction studies. Biopolymers 40:121-39
    • (1996) Biopolymers , vol.40 , pp. 121-139
    • Deschamps, J.R.1    George, C.2    Flippen-Anderson, J.L.3
  • 84
    • 0018144087 scopus 로고
    • Conformation of [Leu5]enkephalin from X-ray diffraction: Features important for recognition at opiate receptor
    • SmithGD, Griffin JF. 1978. Conformation of [Leu5]enkephalin from X-ray diffraction: Features important for recognition at opiate receptor. Science 199:1214-16
    • (1978) Science , vol.199 , pp. 1214-1216
    • Smith, G.D.1    Griffin, J.F.2
  • 85
    • 0032568793 scopus 로고    scopus 로고
    • A critical role for amino-Terminal glutamine/ asparagine repeats in the formation and propagation of a yeast prion
    • DePace AH, Santoso A, Hillner P, Weissman JS. 1998. A critical role for amino-Terminal glutamine/ asparagine repeats in the formation and propagation of a yeast prion. Cell 93:1241-52
    • (1998) Cell , vol.93 , pp. 1241-1252
    • DePace, A.H.1    Santoso, A.2    Hillner, P.3    Weissman, J.S.4
  • 87
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid
    • Balbirnie M, Grothe R, Eisenberg DS. 2001. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA 98:2375-80
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.