메뉴 건너뛰기




Volumn 43, Issue 8, 2008, Pages 1021-1036

Protein structure and dynamics studied by mass spectrometry: H/D exchange, hydroxyl radical labeling, and related approaches

Author keywords

Electrospray ionization; Hydrogen bonds; Protein conformation; Protein folding; Radical scavenger; Solvent exposure; Structural dynamics

Indexed keywords

CHLORINE COMPOUNDS; CONCENTRATION (PROCESS); DOPING (ADDITIVES); DYNAMICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IONIZATION; IONIZATION OF GASES; IONIZATION OF LIQUIDS; ISOTOPES; LABELING; MASS SPECTROMETERS; MASS SPECTROMETRY; PROTEINS; SPECTROMETERS; SPECTROMETRY; SPECTRUM ANALYSIS; STOICHIOMETRY; VACUUM APPLICATIONS;

EID: 49549086897     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1435     Document Type: Review
Times cited : (161)

References (202)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 1973; 181: 223.
    • (1973) Science , vol.181 , pp. 223
    • Anfinsen, C.B.1
  • 2
    • 0025186451 scopus 로고
    • Structural characterisation of a partly folded apomyoglobin intermediate
    • Hughson FM, Wright PE, Baldwin RL. Structural characterisation of a partly folded apomyoglobin intermediate. Science 1990; 249: 1544.
    • (1990) Science , vol.249 , pp. 1544
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 4
    • 0034691233 scopus 로고    scopus 로고
    • Calmodulin-peptide interactions: Apocalmodulin binding to the myosin light chain kinase target site
    • Hill TJ, Lafitte D, Wallace JI, Cooper HJ, Tsvetkov PO, Derrick PJ. Calmodulin-peptide interactions: apocalmodulin binding to the myosin light chain kinase target site. Biochemistry 2000; 39: 7284.
    • (2000) Biochemistry , vol.39 , pp. 7284
    • Hill, T.J.1    Lafitte, D.2    Wallace, J.I.3    Cooper, H.J.4    Tsvetkov, P.O.5    Derrick, P.J.6
  • 5
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright PE, Dyson HJ. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. Journal of Molecular Biology 1999; 293: 321.
    • (1999) Journal of Molecular Biology , vol.293 , pp. 321
    • Wright, P.E.1    Dyson, H.J.2
  • 6
    • 0031851978 scopus 로고    scopus 로고
    • Equilibrium NMR studies of unfolded and partially folded proteins
    • Dyson HJ, Wright PE. Equilibrium NMR studies of unfolded and partially folded proteins. Natural Structural Biology 1998; 5: 499.
    • (1998) Natural Structural Biology , vol.5 , pp. 499
    • Dyson, H.J.1    Wright, P.E.2
  • 8
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase K, Dyson HJ, Wright PE. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 2007; 447: 1021.
    • (2007) Nature , vol.447 , pp. 1021
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 9
    • 36048990877 scopus 로고    scopus 로고
    • Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin α: Evidence for metalation as an entropic switch
    • Yi S, Boys BL, Brickenden A, Konermann L, Choy WY. Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin α: evidence for metalation as an entropic switch. Biochemistry 2007; 46: 13120.
    • (2007) Biochemistry , vol.46 , pp. 13120
    • Yi, S.1    Boys, B.L.2    Brickenden, A.3    Konermann, L.4    Choy, W.Y.5
  • 11
    • 0026320866 scopus 로고
    • The energy landscape and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG. The energy landscape and motions of proteins. Science 1991; 254: 1598.
    • (1991) Science , vol.254 , pp. 1598
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 13
    • 0037154793 scopus 로고    scopus 로고
    • A moving story
    • Falke JJ. A moving story. Science 2002; 295: 1480.
    • (2002) Science , vol.295 , pp. 1480
    • Falke, J.J.1
  • 14
    • 27744480205 scopus 로고    scopus 로고
    • Proteins flex to function
    • Huang YJ, Montelione GT. Proteins flex to function. Nature 2005; 438: 36.
    • (2005) Nature , vol.438 , pp. 36
    • Huang, Y.J.1    Montelione, G.T.2
  • 16
    • 33845184189 scopus 로고    scopus 로고
    • Christianson DW, Lipscomb WN. Carboxypeptidase A. Accounts of Chemical Research 1989; 22: 62.
    • Christianson DW, Lipscomb WN. Carboxypeptidase A. Accounts of Chemical Research 1989; 22: 62.
  • 18
    • 0004091818 scopus 로고    scopus 로고
    • 4th ed. Wm. C. Brown: Dubuque, IA
    • Zubay G. Biochemistry, 4th ed. Wm. C. Brown: Dubuque, IA, 1998; 990.
    • (1998) Biochemistry , pp. 990
    • Zubay, G.1
  • 20
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM. Protein folding and misfolding. Nature 2003; 426: 884.
    • (2003) Nature , vol.426 , pp. 884
    • Dobson, C.M.1
  • 25
    • 0038342516 scopus 로고    scopus 로고
    • Unmasking the annexin I interaction from the structure of apo-S100A11
    • Dempsey AC, Walsh MP, Shaw GS. Unmasking the annexin I interaction from the structure of apo-S100A11. Structure 2003; 11: 887.
    • (2003) Structure , vol.11 , pp. 887
    • Dempsey, A.C.1    Walsh, M.P.2    Shaw, G.S.3
  • 26
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A, Kay LE. New tools provide new insights in NMR studies of protein dynamics. Science 2006; 312: 224.
    • (2006) Science , vol.312 , pp. 224
    • Mittermaier, A.1    Kay, L.E.2
  • 29
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers R, Kay LE. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 2007; 445: 618.
    • (2007) Nature , vol.445 , pp. 618
    • Sprangers, R.1    Kay, L.E.2
  • 30
    • 0041317054 scopus 로고    scopus 로고
    • Electrospray wings for molecular elephants (Nobel Lecture)
    • Fenn JB. Electrospray wings for molecular elephants (Nobel Lecture). Angewandte Chemie International Edition 2003; 42: 3871.
    • (2003) Angewandte Chemie International Edition , vol.42 , pp. 3871
    • Fenn, J.B.1
  • 31
    • 0042318496 scopus 로고    scopus 로고
    • The origin of macromolecule ionization by laser irradiation (Nobel Lecture)
    • Tanaka K. The origin of macromolecule ionization by laser irradiation (Nobel Lecture). Angewandte Chemie International Edition 2003; 42: 3861.
    • (2003) Angewandte Chemie International Edition , vol.42 , pp. 3861
    • Tanaka, K.1
  • 32
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons
    • Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons. Analytical Chemistry 1988; 60: 2299.
    • (1988) Analytical Chemistry , vol.60 , pp. 2299
    • Karas, M.1    Hillenkamp, F.2
  • 40
    • 0242659052 scopus 로고    scopus 로고
    • Bioactive recognition sites may not be energetically preferred in protein-carbohydrate complexes in the gas phase
    • Wang W, Kitova EN, Klassen JS. Bioactive recognition sites may not be energetically preferred in protein-carbohydrate complexes in the gas phase. Journal of the American Chemical Society 2003; 125: 13630.
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 13630
    • Wang, W.1    Kitova, E.N.2    Klassen, J.S.3
  • 42
    • 33750971747 scopus 로고    scopus 로고
    • Top-down ESI-ECD-FT-ICR mass spectrometry localizes noncovalent protein-ligand binding sites
    • Xie Y, Zhang J, Yin S, Loo JA. Top-down ESI-ECD-FT-ICR mass spectrometry localizes noncovalent protein-ligand binding sites. Journal of the American Chemical Society 2006; 128: 14432.
    • (2006) Journal of the American Chemical Society , vol.128 , pp. 14432
    • Xie, Y.1    Zhang, J.2    Yin, S.3    Loo, J.A.4
  • 44
    • 34250161660 scopus 로고    scopus 로고
    • Imaging atomic structure and dynamics wit ultrafast x-ray scattering
    • Gaffney KJ, Chapman HN. Imaging atomic structure and dynamics wit ultrafast x-ray scattering. Science 2007; 316: 1444.
    • (2007) Science , vol.316 , pp. 1444
    • Gaffney, K.J.1    Chapman, H.N.2
  • 48
    • 33845951972 scopus 로고    scopus 로고
    • Gas phase noncovalent protein complexes that retain solution binding properties: Binding of xylobiose inhibitors to the β-1, 4 exoglucanase from Cellulomonas fimi
    • Tesic M, Wicki J, Poon D, Withers KY, Douglas DJ. Gas phase noncovalent protein complexes that retain solution binding properties: binding of xylobiose inhibitors to the β-1, 4 exoglucanase from Cellulomonas fimi. Journal of the American Society for Mass Spectrometry 2007; 18: 64.
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , pp. 64
    • Tesic, M.1    Wicki, J.2    Poon, D.3    Withers, K.Y.4    Douglas, D.J.5
  • 49
    • 23744495939 scopus 로고    scopus 로고
    • The thermal unfolding of native cytochrome c in the transition from solution to gas phase probed by native electron capture dissociation
    • Breuker K, McLafferty FW. The thermal unfolding of native cytochrome c in the transition from solution to gas phase probed by native electron capture dissociation. Angewandte Chemie 2005; 44: 4911.
    • (2005) Angewandte Chemie , vol.44 , pp. 4911
    • Breuker, K.1    McLafferty, F.W.2
  • 50
    • 4444382102 scopus 로고    scopus 로고
    • Probing rhodopsin-transducin interactions by surface modification and mass spectrometry
    • Wang X, Kim S-H, Ablonczy Z, Crouch RK, Knapp DR. Probing rhodopsin-transducin interactions by surface modification and mass spectrometry. Biochemistry 2004; 43: 11153.
    • (2004) Biochemistry , vol.43 , pp. 11153
    • Wang, X.1    Kim, S.-H.2    Ablonczy, Z.3    Crouch, R.K.4    Knapp, D.R.5
  • 52
    • 34547862095 scopus 로고    scopus 로고
    • Expanding the repertoire of an ERK2 recruitment site: Cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding
    • Abramczyk O, Rainey MA, Barnes R, Martin L, Dalby KN. Expanding the repertoire of an ERK2 recruitment site: cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding. Biochemistry 2007; 46: 9174.
    • (2007) Biochemistry , vol.46 , pp. 9174
    • Abramczyk, O.1    Rainey, M.A.2    Barnes, R.3    Martin, L.4    Dalby, K.N.5
  • 53
    • 0037065723 scopus 로고    scopus 로고
    • Characterization of the tertiary structure of soluble CD4 bound to glycosylated full-length HIV gp120 by chemical modification of arginine residues and mass spectrometric analysis
    • Hager-Braun C, Tomer KB. Characterization of the tertiary structure of soluble CD4 bound to glycosylated full-length HIV gp120 by chemical modification of arginine residues and mass spectrometric analysis. Biochemistry 2002; 41: 1759.
    • (2002) Biochemistry , vol.41 , pp. 1759
    • Hager-Braun, C.1    Tomer, K.B.2
  • 54
    • 38049108092 scopus 로고    scopus 로고
    • Exploring the cooperativity of the fast folding reaction of a small protein Using pulsed thiol labeling and mass spectrometry
    • Jha SK, Udgaonkar JB. Exploring the cooperativity of the fast folding reaction of a small protein Using pulsed thiol labeling and mass spectrometry. Journal of Biological Chemistry 2007; 282: 37479.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 37479
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 55
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz A. Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. Journal of Mass Spectrometry 2003; 38: 1225.
    • (2003) Journal of Mass Spectrometry , vol.38 , pp. 1225
    • Sinz, A.1
  • 56
    • 0036558160 scopus 로고    scopus 로고
    • Identification of components of protein complexes using a fluorescent photocross-linker and mass spectrometry
    • Wine RN, Dial JM, Tomer KB, Borchers CH. Identification of components of protein complexes using a fluorescent photocross-linker and mass spectrometry. Analytical Chemistry 2002; 74: 1939.
    • (2002) Analytical Chemistry , vol.74 , pp. 1939
    • Wine, R.N.1    Dial, J.M.2    Tomer, K.B.3    Borchers, C.H.4
  • 57
    • 10644254712 scopus 로고    scopus 로고
    • Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry
    • Vasilescu J, Guo X, Kast J. Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry. Proteomics 2004; 4: 3845.
    • (2004) Proteomics , vol.4 , pp. 3845
    • Vasilescu, J.1    Guo, X.2    Kast, J.3
  • 59
    • 84994982849 scopus 로고
    • Disparity between solution-phase equilibria and charge state distributions in positive-ion electrospray mass spectrometry
    • Wang G, Cole RB. Disparity between solution-phase equilibria and charge state distributions in positive-ion electrospray mass spectrometry. Organic Mass Spectrometry 1994; 29: 419.
    • (1994) Organic Mass Spectrometry , vol.29 , pp. 419
    • Wang, G.1    Cole, R.B.2
  • 60
    • 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. Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes. Journal of the American Society for Mass Spectrometry 1998; 9: 1248.
    • (1998) Journal of the American Society for Mass Spectrometry , vol.9 , pp. 1248
    • Konermann, L.1    Douglas, D.J.2
  • 61
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamics by mass spectrometry
    • Kaltashov IA, Eyles SJ. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrometry Reviews 2002; 21: 37.
    • (2002) Mass Spectrometry Reviews , vol.21 , pp. 37
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 62
    • 0036177471 scopus 로고    scopus 로고
    • Detecting equilibrium cytochrome c folding intermediates by electrospray ionization mass spectrometry: Two partially folded forms populate the molten globule state
    • Grandori R. Detecting equilibrium cytochrome c folding intermediates by electrospray ionization mass spectrometry: two partially folded forms populate the molten globule state. Protein Science 2002; 11: 453.
    • (2002) Protein Science , vol.11 , pp. 453
    • Grandori, R.1
  • 63
    • 0031032512 scopus 로고    scopus 로고
    • Probing subtle acid-induced conformational changes of ribonuclease A by electrospray mass spectrometry
    • Pan XM, Sheng XR, Zhou JM. Probing subtle acid-induced conformational changes of ribonuclease A by electrospray mass spectrometry. FEBS Letters 1997; 402: 25.
    • (1997) FEBS Letters , vol.402 , pp. 25
    • Pan, X.M.1    Sheng, X.R.2    Zhou, J.M.3
  • 64
    • 0034727681 scopus 로고    scopus 로고
    • Methanol-induced conformations of myoglobin at pH 4.0
    • Babu KR, Douglas DJ. Methanol-induced conformations of myoglobin at pH 4.0. Biochemistry 2000; 39: 14702.
    • (2000) Biochemistry , vol.39 , pp. 14702
    • Babu, K.R.1    Douglas, D.J.2
  • 65
    • 0029930590 scopus 로고    scopus 로고
    • Conformational heterogeneity and stability of apomyoglobin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry
    • Wang F, Tang X. Conformational heterogeneity and stability of apomyoglobin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry. Biochemistry 1996; 35: 4069.
    • (1996) Biochemistry , vol.35 , pp. 4069
    • Wang, F.1    Tang, X.2
  • 66
    • 33644663381 scopus 로고    scopus 로고
    • Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange
    • Pan JX, Rintala-Dempsey A, Li Y, Shaw GS, Konermann L. Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange. Biochemistry 2006; 45: 3005.
    • (2006) Biochemistry , vol.45 , pp. 3005
    • Pan, J.X.1    Rintala-Dempsey, A.2    Li, Y.3    Shaw, G.S.4    Konermann, L.5
  • 67
    • 20544458613 scopus 로고    scopus 로고
    • Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments: Implications for ubiquitin Folding
    • Pan JX, Wilson DJ, Konermann L. Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments: implications for ubiquitin Folding. Biochemistry 2005; 44: 8627.
    • (2005) Biochemistry , vol.44 , pp. 8627
    • Pan, J.X.1    Wilson, D.J.2    Konermann, L.3
  • 68
    • 14044268842 scopus 로고    scopus 로고
    • Kinetic unfolding mechanism of the inducible nitric oxide synthase oxygenase domain determined by time-resolved electrospray mass spectrometry
    • Wilson DJ, Rafferty SP, Konermann L. Kinetic unfolding mechanism of the inducible nitric oxide synthase oxygenase domain determined by time-resolved electrospray mass spectrometry. Biochemistry 2005; 44: 2276.
    • (2005) Biochemistry , vol.44 , pp. 2276
    • Wilson, D.J.1    Rafferty, S.P.2    Konermann, L.3
  • 70
    • 0001401150 scopus 로고
    • Observation of the heme-globin complex in native myoglobin by electrospray-ionisation mass spectrometry
    • Katta V, Chait BT. Observation of the heme-globin complex in native myoglobin by electrospray-ionisation mass spectrometry. Journal of the American Chemical Society 1991; 113: 8534.
    • (1991) Journal of the American Chemical Society , vol.113 , pp. 8534
    • Katta, V.1    Chait, B.T.2
  • 71
    • 0037258408 scopus 로고    scopus 로고
    • Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry
    • Grandori R. Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry. Journal of Mass Spectrometry 2003; 38: 11.
    • (2003) Journal of Mass Spectrometry , vol.38 , pp. 11
    • Grandori, R.1
  • 72
    • 58149323703 scopus 로고
    • Intrinsic basicity of oligomeric peptides that contain glycine, alanine, and valine - the effects of the alkyl side chain on proton transfer reactions
    • Wu J, Lebrilla CB. Intrinsic basicity of oligomeric peptides that contain glycine, alanine, and valine - the effects of the alkyl side chain on proton transfer reactions. Journal of the American Society for Mass Spectrometry 1995; 6: 91.
    • (1995) Journal of the American Society for Mass Spectrometry , vol.6 , pp. 91
    • Wu, J.1    Lebrilla, C.B.2
  • 73
    • 0004493005 scopus 로고
    • On the maximum charge state and proton transfer reactivity of peptide and protein ions formed by electrospray ionization
    • Schnier PD, Gross DS, Williams ER. On the maximum charge state and proton transfer reactivity of peptide and protein ions formed by electrospray ionization. Journal of the American Society for Mass Spectrometry 1995; 6: 1086.
    • (1995) Journal of the American Society for Mass Spectrometry , vol.6 , pp. 1086
    • Schnier, P.D.1    Gross, D.S.2    Williams, E.R.3
  • 74
    • 0141458006 scopus 로고    scopus 로고
    • Role of opposite charge in protein electrospray ionization mass spectrometry
    • Samalikova M, Grandori R. Role of opposite charge in protein electrospray ionization mass spectrometry. Journal of Mass Spectrometry 2003; 38: 941.
    • (2003) Journal of Mass Spectrometry , vol.38 , pp. 941
    • Samalikova, M.1    Grandori, R.2
  • 75
    • 23744516059 scopus 로고    scopus 로고
    • Estimates of protein surface area in solution by electrospray ionization mass spectrometry
    • Kaltashov IA, Mohimen A. Estimates of protein surface area in solution by electrospray ionization mass spectrometry. Analytical Chemistry 2005; 77: 5370.
    • (2005) Analytical Chemistry , vol.77 , pp. 5370
    • Kaltashov, I.A.1    Mohimen, A.2
  • 76
    • 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
    • Konermann L, Douglas DJ. 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
  • 77
    • 34347332295 scopus 로고    scopus 로고
    • A minimalist model for exploring conformational effects on the electrospray charge state distribution of proteins
    • Konermann L. A minimalist model for exploring conformational effects on the electrospray charge state distribution of proteins. Journal of Physical Chemistry B 2007; 111: 6534.
    • (2007) Journal of Physical Chemistry B , vol.111 , pp. 6534
    • Konermann, L.1
  • 79
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • Robinson CV, Sali A, Baumeister W. The molecular sociology of the cell. Nature 2007; 450: 973.
    • (2007) Nature , vol.450 , pp. 973
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 81
    • 23744481400 scopus 로고    scopus 로고
    • What do we learn from high-throughput protein interaction data?
    • Titz B, Schlesner M, Uetz P. What do we learn from high-throughput protein interaction data? Expert Review of Proteomics 2004; 1: 111.
    • (2004) Expert Review of Proteomics , vol.1 , pp. 111
    • Titz, B.1    Schlesner, M.2    Uetz, P.3
  • 82
    • 3342925849 scopus 로고    scopus 로고
    • Methods to study protein dynamics and folding by mass spectrometry
    • Eyles SJ, Kaltashov IA. Methods to study protein dynamics and folding by mass spectrometry. Methods 2004; 34: 88.
    • (2004) Methods , vol.34 , pp. 88
    • Eyles, S.J.1    Kaltashov, I.A.2
  • 83
    • 0041471397 scopus 로고    scopus 로고
    • Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry
    • Griffith WP, Kaltashov IA. Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry. Biochemistry 2003; 42: 10024.
    • (2003) Biochemistry , vol.42 , pp. 10024
    • Griffith, W.P.1    Kaltashov, I.A.2
  • 84
    • 0037065802 scopus 로고    scopus 로고
    • Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-line isotopic pulse labeling
    • Simmons DA, Konermann L. Characterization of transient protein folding intermediates during myoglobin reconstitution by time-resolved electrospray mass spectrometry with on-line isotopic pulse labeling. Biochemistry 2002; 41: 1906.
    • (2002) Biochemistry , vol.41 , pp. 1906
    • Simmons, D.A.1    Konermann, L.2
  • 85
    • 34548768193 scopus 로고    scopus 로고
    • Symmetric behaviour of hemoglobin α- and β- subunits during acid-induced denaturation observed by electrospray mass spectrometry
    • Boys BL, Kuprowski MC, Konermann L. Symmetric behaviour of hemoglobin α- and β- subunits during acid-induced denaturation observed by electrospray mass spectrometry. Biochemistry 2007; 46: 10675.
    • (2007) Biochemistry , vol.46 , pp. 10675
    • Boys, B.L.1    Kuprowski, M.C.2    Konermann, L.3
  • 86
    • 0000273962 scopus 로고
    • Stepwise refolding of acid-denatured myoglobin: Evidence from electrospray mass spectrometry
    • Feng R, Konishi Y. Stepwise refolding of acid-denatured myoglobin: evidence from electrospray mass spectrometry. Journal of the American Society for Mass Spectrometry 1993; 4: 638.
    • (1993) Journal of the American Society for Mass Spectrometry , vol.4 , pp. 638
    • Feng, R.1    Konishi, Y.2
  • 87
    • 0031213609 scopus 로고    scopus 로고
    • Investigation of calcium-induced, noncovalent association of calmodulin with melittin by electrospray ionization mass spectrometry
    • Nemirovskiy OV, Ramanathan R, Gross ML. Investigation of calcium-induced, noncovalent association of calmodulin with melittin by electrospray ionization mass spectrometry. Journal of the American Society for Mass Spectrometry 1997; 8: 809.
    • (1997) Journal of the American Society for Mass Spectrometry , vol.8 , pp. 809
    • Nemirovskiy, O.V.1    Ramanathan, R.2    Gross, M.L.3
  • 88
    • 0032125821 scopus 로고    scopus 로고
    • Detection of a monomeric intermediate associated with dimerization of protein Hu by mass spectrometry
    • Vis H, Heinemann U, Dobson CM, Robinson CV. Detection of a monomeric intermediate associated with dimerization of protein Hu by mass spectrometry. Journal of the American Chemical Society 1998; 120: 6427.
    • (1998) Journal of the American Chemical Society , vol.120 , pp. 6427
    • Vis, H.1    Heinemann, U.2    Dobson, C.M.3    Robinson, C.V.4
  • 91
    • 34548215681 scopus 로고    scopus 로고
    • Protein complexes in the gas phase: Technology for structural genomics and proteomics
    • Benesch JLP, Ruotolo BT, Simmons DA, Robinson CV. Protein complexes in the gas phase: technology for structural genomics and proteomics. Chemical Reviews 2007; 107: 3544.
    • (2007) Chemical Reviews , vol.107 , pp. 3544
    • Benesch, J.L.P.1    Ruotolo, B.T.2    Simmons, D.A.3    Robinson, C.V.4
  • 93
    • 1442348875 scopus 로고    scopus 로고
    • Screening for noncovalent ligand-receptor interactions by electrospray ionization mass spectrometry-based diffusion measurements
    • Clark SM, Konermann L. Screening for noncovalent ligand-receptor interactions by electrospray ionization mass spectrometry-based diffusion measurements. Analytical Chemistry 2004; 76: 1257.
    • (2004) Analytical Chemistry , vol.76 , pp. 1257
    • Clark, S.M.1    Konermann, L.2
  • 94
    • 10044271179 scopus 로고    scopus 로고
    • Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements
    • Clark SM, Konermann L. Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements. Analytical Chemistry 2004; 76: 7077.
    • (2004) Analytical Chemistry , vol.76 , pp. 7077
    • Clark, S.M.1    Konermann, L.2
  • 95
    • 33846194221 scopus 로고    scopus 로고
    • Method for stabilizing protein-ligand complexes in nanoelectrospray ionization mass spectrometry
    • Sun J, Kitova EN, Klassen JS. Method for stabilizing protein-ligand complexes in nanoelectrospray ionization mass spectrometry. Analytical Chemistry 2007; 79: 416.
    • (2007) Analytical Chemistry , vol.79 , pp. 416
    • Sun, J.1    Kitova, E.N.2    Klassen, J.S.3
  • 96
    • 35848941191 scopus 로고    scopus 로고
    • Method for identifying nonspecific protein-protein interactions in nanoelectrospray ionization mass spectrometry
    • Sun J, Kitova EN, Sun N, Klassen JS. Method for identifying nonspecific protein-protein interactions in nanoelectrospray ionization mass spectrometry. Analytical Chemistry 2007; 79: 8301.
    • (2007) Analytical Chemistry , vol.79 , pp. 8301
    • Sun, J.1    Kitova, E.N.2    Sun, N.3    Klassen, J.S.4
  • 97
    • 4744344760 scopus 로고    scopus 로고
    • Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method
    • Peschke M, Verkerk UH, Kebarle P. Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method. Journal of the American Society for Mass Spectrometry 2004; 15: 1424.
    • (2004) Journal of the American Society for Mass Spectrometry , vol.15 , pp. 1424
    • Peschke, M.1    Verkerk, U.H.2    Kebarle, P.3
  • 99
    • 33947377924 scopus 로고    scopus 로고
    • Signal response of co-existing protein conformers in electrospray mass spectrometry
    • Kuprowski MC, Konermann L. Signal response of co-existing protein conformers in electrospray mass spectrometry. Analytical Chemistry 2007; 79: 2499.
    • (2007) Analytical Chemistry , vol.79 , pp. 2499
    • Kuprowski, M.C.1    Konermann, L.2
  • 100
    • 0037941316 scopus 로고    scopus 로고
    • Influence of response factors on determining equilibrium association constants of non-covalent complexes by electrospray ionization mass spectrometry
    • Gabelica V, Galic N, Rosu F, Houssier C, De Pauw E. Influence of response factors on determining equilibrium association constants of non-covalent complexes by electrospray ionization mass spectrometry. Journal of Mass Spectrometry 2003; 38: 491.
    • (2003) Journal of Mass Spectrometry , vol.38 , pp. 491
    • Gabelica, V.1    Galic, N.2    Rosu, F.3    Houssier, C.4    De Pauw, E.5
  • 101
    • 0141958921 scopus 로고    scopus 로고
    • Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry
    • Wang W, Kitova EN, Klassen JS. Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry. Analytical Chemistry 2003; 75: 4945.
    • (2003) Analytical Chemistry , vol.75 , pp. 4945
    • Wang, W.1    Kitova, E.N.2    Klassen, J.S.3
  • 102
    • 0032532125 scopus 로고    scopus 로고
    • Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry
    • Jørgensen TJD, Roepstorff P, Heck AJR. Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry. Analytical Chemistry 1998; 70: 4427.
    • (1998) Analytical Chemistry , vol.70 , pp. 4427
    • Jørgensen, T.J.D.1    Roepstorff, P.2    Heck, A.J.R.3
  • 103
    • 0034716184 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: A technology for studying noncovalent macromolecular complexes
    • Loo JA. Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes. International Journal of Mass Spectrometry 2000; 200: 175.
    • (2000) International Journal of Mass Spectrometry , vol.200 , pp. 175
    • Loo, J.A.1
  • 104
    • 11844260047 scopus 로고    scopus 로고
    • Instrumental parameters in the maldi-tof mass spectrometric analysis of quaternary protein structures
    • Zehl M, Allmaier G. Instrumental parameters in the maldi-tof mass spectrometric analysis of quaternary protein structures. Analytical Chemistry 2005; 77: 103.
    • (2005) Analytical Chemistry , vol.77 , pp. 103
    • Zehl, M.1    Allmaier, G.2
  • 106
  • 111
    • 0242579199 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry of actin in various biochemical contexts
    • Chik JK, Schriemer DC. Hydrogen/deuterium exchange mass spectrometry of actin in various biochemical contexts. Journal of Molecular Biology 2003; 334: 373.
    • (2003) Journal of Molecular Biology , vol.334 , pp. 373
    • Chik, J.K.1    Schriemer, D.C.2
  • 115
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales TE, Engen JR. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrometry Reviews 2006; 25: 158.
    • (2006) Mass Spectrometry Reviews , vol.25 , pp. 158
    • Wales, T.E.1    Engen, J.R.2
  • 116
    • 0038293125 scopus 로고    scopus 로고
    • Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX
    • Zhu MM, Rempel DL, Du Z, Gross ML. Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX. Journal of the American Chemical Society 2003; 125: 5252.
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 5252
    • Zhu, M.M.1    Rempel, D.L.2    Du, Z.3    Gross, M.L.4
  • 119
    • 0037614815 scopus 로고    scopus 로고
    • Conformational dynamics of partially denatured myoglobin studied by time-resolved electrospray mass spectrometry with online hydrogen-deuterium exchange
    • Simmons DA, Dunn SD, Konermann L. Conformational dynamics of partially denatured myoglobin studied by time-resolved electrospray mass spectrometry with online hydrogen-deuterium exchange. Biochemistry 2003; 42: 5896.
    • (2003) Biochemistry , vol.42 , pp. 5896
    • Simmons, D.A.1    Dunn, S.D.2    Konermann, L.3
  • 120
    • 1842868694 scopus 로고    scopus 로고
    • Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes
    • Yan X, Watson J, Ho PS, Deinzer ML. Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes. Molecular and Cellular Proteomics 2004; 3: 10.
    • (2004) Molecular and Cellular Proteomics , vol.3 , pp. 10
    • Yan, X.1    Watson, J.2    Ho, P.S.3    Deinzer, M.L.4
  • 121
    • 0031018084 scopus 로고    scopus 로고
    • Probing the noncovalent structure of proteins by amide hydrogen exchange mass spectrometry
    • Smith DL, Deng Y, Zhang Z. Probing the noncovalent structure of proteins by amide hydrogen exchange mass spectrometry. Journal of Mass Spectrometry 1997; 32: 135.
    • (1997) Journal of Mass Spectrometry , vol.32 , pp. 135
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 122
    • 0035326304 scopus 로고    scopus 로고
    • Investigating protein structure and dynamics by hydrogen exchange MS
    • Engen JR, Smith DL. Investigating protein structure and dynamics by hydrogen exchange MS. Analytical Chemistry 2001; 73: 256A.
    • (2001) Analytical Chemistry , vol.73
    • Engen, J.R.1    Smith, D.L.2
  • 123
    • 30344476997 scopus 로고    scopus 로고
    • Protein conformations, interactions, and H/D exchange
    • Maier CS, Deinzer ML. Protein conformations, interactions, and H/D exchange. Methods in Enzymology 2005; 402: 312.
    • (2005) Methods in Enzymology , vol.402 , pp. 312
    • Maier, C.S.1    Deinzer, M.L.2
  • 125
    • 13244258262 scopus 로고    scopus 로고
    • Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment
    • Xiao H, Hoerner JK, Eyles SJ, Dobo A, Voigtman E, Melcuk AI, Kaltashov IA. Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two-state protein and comparison with experiment. Protein Science 2005; 14: 543.
    • (2005) Protein Science , vol.14 , pp. 543
    • Xiao, H.1    Hoerner, J.K.2    Eyles, S.J.3    Dobo, A.4    Voigtman, E.5    Melcuk, A.I.6    Kaltashov, I.A.7
  • 126
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • Roder H, Elöve GA, Englander SW. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature 1988; 335: 700.
    • (1988) Nature , vol.335 , pp. 700
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 127
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • Udgaonkar JB, Baldwin RL. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature 1988; 335: 694.
    • (1988) Nature , vol.335 , pp. 694
    • Udgaonkar, J.B.1    Baldwin, R.L.2
  • 128
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules under native conditions
    • Raschke TM, Marqusee S. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules under native conditions. Natural Structural Biology 1997; 4: 298.
    • (1997) Natural Structural Biology , vol.4 , pp. 298
    • Raschke, T.M.1    Marqusee, S.2
  • 129
    • 0030780768 scopus 로고    scopus 로고
    • Kinetics of cytochrome c folding examined by hydrogen exchange and mass spectrometry
    • Yang H, Smith DL. Kinetics of cytochrome c folding examined by hydrogen exchange and mass spectrometry. Biochemistry 1997; 36: 14992.
    • (1997) Biochemistry , vol.36 , pp. 14992
    • Yang, H.1    Smith, D.L.2
  • 130
    • 0032901420 scopus 로고    scopus 로고
    • Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate
    • Tsui V, Garcia C, Cavagnero S, Siuzdak G, Dyson HJ, Wright PE. Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate. Protein Science 1999; 8: 45.
    • (1999) Protein Science , vol.8 , pp. 45
    • Tsui, V.1    Garcia, C.2    Cavagnero, S.3    Siuzdak, G.4    Dyson, H.J.5    Wright, P.E.6
  • 132
    • 0038271924 scopus 로고    scopus 로고
    • Protein folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry
    • Konermann L, Simmons DA. Protein folding kinetics and mechanisms studied by pulse-labeling and mass spectrometry. Mass Spectrometry Reviews 2003; 22: 1.
    • (2003) Mass Spectrometry Reviews , vol.22 , pp. 1
    • Konermann, L.1    Simmons, D.A.2
  • 133
    • 0034725549 scopus 로고    scopus 로고
    • A statistical appraisal of native state hydrogen exchange data: Evidence for a burst phase continuum?
    • Parker MJ, Marqusee S. A statistical appraisal of native state hydrogen exchange data: evidence for a burst phase continuum? Journal of Molecular Biology 2000; 300: 1361.
    • (2000) Journal of Molecular Biology , vol.300 , pp. 1361
    • Parker, M.J.1    Marqusee, S.2
  • 134
  • 135
    • 0028609035 scopus 로고
    • Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holomyoglobin
    • Johnson RS, Walsh KA. Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holomyoglobin. Protein Science 1994; 3: 2411.
    • (1994) Protein Science , vol.3 , pp. 2411
    • Johnson, R.S.1    Walsh, K.A.2
  • 137
    • 33644781734 scopus 로고    scopus 로고
    • Extensive deuterium back-exchange in certain immobilized pepsin columns used for H/D exchange mass spectrometry
    • Wu Y, Kaveti S, Engen JR. Extensive deuterium back-exchange in certain immobilized pepsin columns used for H/D exchange mass spectrometry. Analytical Chemistry 2006; 78: 1719.
    • (2006) Analytical Chemistry , vol.78 , pp. 1719
    • Wu, Y.1    Kaveti, S.2    Engen, J.R.3
  • 138
    • 2942650157 scopus 로고    scopus 로고
    • Is there hydrogen scrambling in the gas phase? Energetic and structural determinants of proton mobility within protein ions
    • Hoerner JK, Xiao H, Dobo A, Kaltashov IA. Is there hydrogen scrambling in the gas phase? Energetic and structural determinants of proton mobility within protein ions. Journal of the American Chemical Society 2004; 126: 7709.
    • (2004) Journal of the American Chemical Society , vol.126 , pp. 7709
    • Hoerner, J.K.1    Xiao, H.2    Dobo, A.3    Kaltashov, I.A.4
  • 139
    • 38649092998 scopus 로고    scopus 로고
    • Electron capture dissociation proceeds with a low degree of intramolecular migration of peptide amide hydrogens
    • Rand KD, Adams CM, Zubarev RA, Jorgensen TJD. Electron capture dissociation proceeds with a low degree of intramolecular migration of peptide amide hydrogens. Journal of the American Chemical Society 2008; 130: 1341.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 1341
    • Rand, K.D.1    Adams, C.M.2    Zubarev, R.A.3    Jorgensen, T.J.D.4
  • 143
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander SW, Kallenbach NR. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quarterly Review of Biophysics 1984; 16: 521.
    • (1984) Quarterly Review of Biophysics , vol.16 , pp. 521
    • Englander, S.W.1    Kallenbach, N.R.2
  • 144
    • 35648957285 scopus 로고    scopus 로고
    • Scope and utility of hydrogen exchange as a tool for mapping landscapes
    • Jaswal SS, Miranker AD. Scope and utility of hydrogen exchange as a tool for mapping landscapes. Protein Science 2007; 16: 2378.
    • (2007) Protein Science , vol.16 , pp. 2378
    • Jaswal, S.S.1    Miranker, A.D.2
  • 146
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW. Protein folding intermediates: native state hydrogen exchange. Science 1995; 269: 192.
    • (1995) Science , vol.269 , pp. 192
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 150
    • 0037133181 scopus 로고    scopus 로고
    • Native state EX2 and EX1 hydrogen exchange of Escherichia coli CspA, a small β-sheet protein
    • Rodriguez HM, Robertson AD, Gregoret LM. Native state EX2 and EX1 hydrogen exchange of Escherichia coli CspA, a small β-sheet protein. Biochemistry 2002; 41: 2140.
    • (2002) Biochemistry , vol.41 , pp. 2140
    • Rodriguez, H.M.1    Robertson, A.D.2    Gregoret, L.M.3
  • 152
    • 0033579918 scopus 로고    scopus 로고
    • Thermal denaturation of Escherichia coli thioredoxin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry: Monitoring a two-state protein unfolding transition
    • Maier CS, Schimerlik MI, Deinzer ML. Thermal denaturation of Escherichia coli thioredoxin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry: monitoring a two-state protein unfolding transition. Biochemistry 1999; 38: 1136.
    • (1999) Biochemistry , vol.38 , pp. 1136
    • Maier, C.S.1    Schimerlik, M.I.2    Deinzer, M.L.3
  • 153
    • 33748280491 scopus 로고    scopus 로고
    • Exploring the relationship between funneled energy landscapes and two-state protein folding
    • Konermann L. Exploring the relationship between funneled energy landscapes and two-state protein folding. Proteins 2006; 65: 153.
    • (2006) Proteins , vol.65 , pp. 153
    • Konermann, L.1
  • 155
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim K-S, Woodward C. Protein internal flexibility and global stability: effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 1993; 32: 9609.
    • (1993) Biochemistry , vol.32 , pp. 9609
    • Kim, K.-S.1    Woodward, C.2
  • 156
    • 0031662891 scopus 로고    scopus 로고
    • Evidence for an unfolding and refolding pathway in cytochrome c
    • Xu Y, Mayne L, Englander SW. Evidence for an unfolding and refolding pathway in cytochrome c. Nature Structural Biology 1998; 5: 774.
    • (1998) Nature Structural Biology , vol.5 , pp. 774
    • Xu, Y.1    Mayne, L.2    Englander, S.W.3
  • 157
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain AK, Handel TM, Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Structural Biology 1996; 3: 782.
    • (1996) Nature Structural Biology , vol.3 , pp. 782
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 158
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: The modern legacy of Linderstrøm-Lang
    • Englander SW, Bai LM, Sosnick TR. Hydrogen exchange: the modern legacy of Linderstrøm-Lang. Protein Science 1997; 6: 1101.
    • (1997) Protein Science , vol.6 , pp. 1101
    • Englander, S.W.1    Bai, L.M.2    Sosnick, T.R.3
  • 163
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • Takamono K, Chance MR. Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Annual Review of Biophysics and Biomolecular Structure 2006; 35: 251.
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 251
    • Takamono, K.1    Chance, M.R.2
  • 164
    • 0035497782 scopus 로고    scopus 로고
    • Radical approaches to probe protein structure, folding, and interactions by mass spectrometry
    • Maleknia SD, Downard K. Radical approaches to probe protein structure, folding, and interactions by mass spectrometry. Mass Spectrometry Reviews 2001; 20: 388.
    • (2001) Mass Spectrometry Reviews , vol.20 , pp. 388
    • Maleknia, S.D.1    Downard, K.2
  • 165
    • 33750632747 scopus 로고    scopus 로고
    • Laser flash photochemical oxidation to locate heme binding and conformational changes in myoglobin
    • Hambly DM, Gross MJ. Laser flash photochemical oxidation to locate heme binding and conformational changes in myoglobin. International Journal of Mass Spectrometry 2007; 259: 124.
    • (2007) International Journal of Mass Spectrometry , vol.259 , pp. 124
    • Hambly, D.M.1    Gross, M.J.2
  • 166
    • 0037442729 scopus 로고    scopus 로고
    • Protein surface mapping by chemical oxidation: Structural analysis by mass spectrometry
    • Sharp JS, Becker JM, Hettich RL. Protein surface mapping by chemical oxidation: structural analysis by mass spectrometry. Analytical Biochemistry 2003; 313: 216.
    • (2003) Analytical Biochemistry , vol.313 , pp. 216
    • Sharp, J.S.1    Becker, J.M.2    Hettich, R.L.3
  • 167
    • 0037353826 scopus 로고    scopus 로고
    • Development of a methodology based on metal-catalyzed oxidation reactions and mass spectrometry to determine the metal binding sites in copper metalloproteins
    • Lim J, Vachet RW. Development of a methodology based on metal-catalyzed oxidation reactions and mass spectrometry to determine the metal binding sites in copper metalloproteins. Analytical Chemistry 2003; 75: 1164.
    • (2003) Analytical Chemistry , vol.75 , pp. 1164
    • Lim, J.1    Vachet, R.W.2
  • 168
    • 33646864750 scopus 로고    scopus 로고
    • Measurement of multisite oxidation kinetics reveals an active site conformational change in spo0f as a result of protein oxidation
    • Sharp JS, Sullivan DM, Cavanagh J, Tomer KB. Measurement of multisite oxidation kinetics reveals an active site conformational change in spo0f as a result of protein oxidation. Biochemistry 2006; 45: 6260.
    • (2006) Biochemistry , vol.45 , pp. 6260
    • Sharp, J.S.1    Sullivan, D.M.2    Cavanagh, J.3    Tomer, K.B.4
  • 169
    • 34548337296 scopus 로고    scopus 로고
    • Hydroxyl radical-mediated modification of proteins as probes for structural proteomics
    • Xu G, Chance MR. Hydroxyl radical-mediated modification of proteins as probes for structural proteomics. Chemical Reviews 2007; 107: 3514.
    • (2007) Chemical Reviews , vol.107 , pp. 3514
    • Xu, G.1    Chance, M.R.2
  • 170
    • 0037603213 scopus 로고    scopus 로고
    • COMPLX: A computer algorithm for the detection of protein-ligand and other macromolecular complexes in mass spectra
    • Wong JWH, Downard KM. COMPLX: a computer algorithm for the detection of protein-ligand and other macromolecular complexes in mass spectra. Journal of Mass Spectrometry 2003; 38: 573.
    • (2003) Journal of Mass Spectrometry , vol.38 , pp. 573
    • Wong, J.W.H.1    Downard, K.M.2
  • 171
    • 0242500901 scopus 로고    scopus 로고
    • Study of the ribunuclease-s-protein- peptide complex using a radical probe and electrospray ionization mass spectrometry
    • Wong JWH, Maleknia SD, Downard KM. Study of the ribunuclease-s-protein- peptide complex using a radical probe and electrospray ionization mass spectrometry. Analytical Chemistry 2003; 75: 1557.
    • (2003) Analytical Chemistry , vol.75 , pp. 1557
    • Wong, J.W.H.1    Maleknia, S.D.2    Downard, K.M.3
  • 172
    • 13444309381 scopus 로고    scopus 로고
    • Hydroxyl radical probe of the calmodulin-melittin complex interface by electrospray ionization mass spectrometry
    • Wong JWH, Maleknia SD, Downard KM. Hydroxyl radical probe of the calmodulin-melittin complex interface by electrospray ionization mass spectrometry. Journal of the American Society for Mass Spectrometry 2005; 16: 225.
    • (2005) Journal of the American Society for Mass Spectrometry , vol.16 , pp. 225
    • Wong, J.W.H.1    Maleknia, S.D.2    Downard, K.M.3
  • 173
    • 33747889776 scopus 로고    scopus 로고
    • PROXIMO - a new docking algorithm to model protein complexes using data from radical probe mass spectrometry (RP-MS)
    • Gerega SK, Downard KM. PROXIMO - a new docking algorithm to model protein complexes using data from radical probe mass spectrometry (RP-MS). Bioinformatics 2006; 22: 1702.
    • (2006) Bioinformatics , vol.22 , pp. 1702
    • Gerega, S.K.1    Downard, K.M.2
  • 174
    • 0037035538 scopus 로고    scopus 로고
    • Mapping the G-Actin binding surface of cofilin using synchrotron protein footprinting
    • Guan JQ, Vorobiev S, Almo SC, Chance MR. Mapping the G-Actin binding surface of cofilin using synchrotron protein footprinting. Biochemistry 2002; 41: 5765.
    • (2002) Biochemistry , vol.41 , pp. 5765
    • Guan, J.Q.1    Vorobiev, S.2    Almo, S.C.3    Chance, M.R.4
  • 175
    • 0036006581 scopus 로고    scopus 로고
    • Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry
    • Maleknia SD, Kiselar JG, Downard KM. Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry. Rapid Communications in Mass Spectrometry 2002; 16: 53.
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , pp. 53
    • Maleknia, S.D.1    Kiselar, J.G.2    Downard, K.M.3
  • 176
    • 0842283944 scopus 로고    scopus 로고
    • Analysis of protein solvent accessible surfaces by photochemical oxidation and mass spectrometry
    • Sharp JS, Becker JM, Hettich RL. Analysis of protein solvent accessible surfaces by photochemical oxidation and mass spectrometry. Analytical Chemistry 2004; 76: 672.
    • (2004) Analytical Chemistry , vol.76 , pp. 672
    • Sharp, J.S.1    Becker, J.M.2    Hettich, R.L.3
  • 178
    • 24944566705 scopus 로고    scopus 로고
    • Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry
    • Aye TT, Low TY, Sze SK. Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry. Analytical Chemistry 2005; 77: 5814.
    • (2005) Analytical Chemistry , vol.77 , pp. 5814
    • Aye, T.T.1    Low, T.Y.2    Sze, S.K.3
  • 179
    • 27844593258 scopus 로고    scopus 로고
    • Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale
    • Hambly DM, Gross MJ. Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale. Journal of the American Society for Mass Spectrometry 2005; 16: 2057.
    • (2005) Journal of the American Society for Mass Spectrometry , vol.16 , pp. 2057
    • Hambly, D.M.1    Gross, M.J.2
  • 180
    • 33645660374 scopus 로고    scopus 로고
    • Transition metal-peptide binding studied by metal-catalyzed oxidation reactions and mass spectrometry
    • Bridgewater JD, Lim J, Vachet RW. Transition metal-peptide binding studied by metal-catalyzed oxidation reactions and mass spectrometry. Analytical Chemistry 2006; 78: 2432.
    • (2006) Analytical Chemistry , vol.78 , pp. 2432
    • Bridgewater, J.D.1    Lim, J.2    Vachet, R.W.3
  • 181
    • 0033568535 scopus 로고    scopus 로고
    • Millisecond radiolytic modification of peptides by synchrotron x-rays identified by mass spectrometry
    • Maleknia SD, Brenowitz M, Chance MR. Millisecond radiolytic modification of peptides by synchrotron x-rays identified by mass spectrometry. Analytical Chemistry 1999; 71: 3965.
    • (1999) Analytical Chemistry , vol.71 , pp. 3965
    • Maleknia, S.D.1    Brenowitz, M.2    Chance, M.R.3
  • 182
    • 33847794081 scopus 로고    scopus 로고
    • Analysis of the oxidative damage-induced conformational changes of Apo- and holocalmodulin by dose-dependent protein oxidative surface mapping
    • Sharp JS, Tomer KB. Analysis of the oxidative damage-induced conformational changes of Apo- and holocalmodulin by dose-dependent protein oxidative surface mapping. Biophysical Journal 2007; 92: 1682.
    • (2007) Biophysical Journal , vol.92 , pp. 1682
    • Sharp, J.S.1    Tomer, K.B.2
  • 184
    • 34548048810 scopus 로고    scopus 로고
    • Effects of protein concentration on the extent of γ-ray-mediated oxidative labeling studied by electrospray mass spectrometry
    • Tong X, Wren JC, Konermann L. Effects of protein concentration on the extent of γ-ray-mediated oxidative labeling studied by electrospray mass spectrometry. Analytical Chemistry 2007; 79: 6376.
    • (2007) Analytical Chemistry , vol.79 , pp. 6376
    • Tong, X.1    Wren, J.C.2    Konermann, L.3
  • 185
    • 0348014523 scopus 로고    scopus 로고
    • Radiolytic modification of basic amino acid residues in peptides: Probes for examining protein-protein interactions
    • Xu G, Takamoto K, Chance MR. Radiolytic modification of basic amino acid residues in peptides: probes for examining protein-protein interactions. Analytical Chemistry 2003; 75: 6995.
    • (2003) Analytical Chemistry , vol.75 , pp. 6995
    • Xu, G.1    Takamoto, K.2    Chance, M.R.3
  • 187
    • 84918833988 scopus 로고
    • Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals (.OH/.O) in aqueous solution
    • Buxton GV, Greenstock CL, Helman WP, Ross AB. Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals (.OH/.O) in aqueous solution. Journal of Physical and Chemical Reference Data 1988; 17: 513.
    • (1988) Journal of Physical and Chemical Reference Data , vol.17 , pp. 513
    • Buxton, G.V.1    Greenstock, C.L.2    Helman, W.P.3    Ross, A.B.4
  • 188
    • 0035086071 scopus 로고    scopus 로고
    • LIRIC 3.2 an updated moded for iodine behavior in the presence of organic impurities
    • Wren JC, Ball JM. LIRIC 3.2 an updated moded for iodine behavior in the presence of organic impurities. Radiation Physics and Chemistry 2001; 60: 577.
    • (2001) Radiation Physics and Chemistry , vol.60 , pp. 577
    • Wren, J.C.1    Ball, J.M.2
  • 189
    • 0028820703 scopus 로고    scopus 로고
    • Myers JK, Pace CN, Schotz JM. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Science 1995; 4: 2138.
    • Myers JK, Pace CN, Schotz JM. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Science 1995; 4: 2138.
  • 190
    • 1442299864 scopus 로고    scopus 로고
    • Radiolytic modification of acidic amino acid residues in peptides: Probes for examining protein-protein interactions
    • Xu G, Chance MR. Radiolytic modification of acidic amino acid residues in peptides: probes for examining protein-protein interactions. Analytical Chemistry 2004; 76: 1213.
    • (2004) Analytical Chemistry , vol.76 , pp. 1213
    • Xu, G.1    Chance, M.R.2
  • 191
    • 18844415551 scopus 로고    scopus 로고
    • Secondary reactions and strategies to improve quantitative protein footprinting
    • Xu G, Kiselar J, He Q, Chance MR. Secondary reactions and strategies to improve quantitative protein footprinting. Analytical Chemistry 2005; 77: 3029.
    • (2005) Analytical Chemistry , vol.77 , pp. 3029
    • Xu, G.1    Kiselar, J.2    He, Q.3    Chance, M.R.4
  • 192
    • 25144465204 scopus 로고    scopus 로고
    • Radiolytic modification and reactivity of amino acid residues as structural probes for protein footprinting
    • Xu G, Chance MR. Radiolytic modification and reactivity of amino acid residues as structural probes for protein footprinting. Analytical Chemistry 2005; 77: 4549.
    • (2005) Analytical Chemistry , vol.77 , pp. 4549
    • Xu, G.1    Chance, M.R.2
  • 193
    • 17644406754 scopus 로고    scopus 로고
    • Radiolytic modification of sulfur-containing amino acid residues in model peptides: Fundamental studies for protein footprinting
    • Xu G, Chance MR. Radiolytic modification of sulfur-containing amino acid residues in model peptides: fundamental studies for protein footprinting. Analytical Chemistry 2005; 77: 2437.
    • (2005) Analytical Chemistry , vol.77 , pp. 2437
    • Xu, G.1    Chance, M.R.2
  • 194
    • 4644253428 scopus 로고    scopus 로고
    • Photochemical and electiophysical production of radicals on millisecond timescales to probe the structure, dynamics, and interactions of proteins
    • Maleknia SD, Wong JWH, Downard KM. Photochemical and electiophysical production of radicals on millisecond timescales to probe the structure, dynamics, and interactions of proteins. Photochemical and Photobiological Sciences 2004; 3: 741.
    • (2004) Photochemical and Photobiological Sciences , vol.3 , pp. 741
    • Maleknia, S.D.1    Wong, J.W.H.2    Downard, K.M.3
  • 196
    • 0035719748 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry
    • Maleknia SD, Downard KM. Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry. European Journal of Biochemistry 2001; 268: 5578.
    • (2001) European Journal of Biochemistry , vol.268 , pp. 5578
    • Maleknia, S.D.1    Downard, K.M.2
  • 198
    • 33750632747 scopus 로고    scopus 로고
    • Laser flash photochemical oxidation to locate heme binding and conformational changes in myoglobin
    • Hambly DM, Gross M. Laser flash photochemical oxidation to locate heme binding and conformational changes in myoglobin. International Journal of Mass Spectrometry 2007; 259: 124.
    • (2007) International Journal of Mass Spectrometry , vol.259 , pp. 124
    • Hambly, D.M.1    Gross, M.2
  • 199
    • 41449103552 scopus 로고    scopus 로고
    • γ-ray-mediated oxidative labeling for detecting protein conformational changes by electrospray mass spectrometry
    • Tong X, Wren JC, Konermann L. γ-ray-mediated oxidative labeling for detecting protein conformational changes by electrospray mass spectrometry. Analytical Chemistry 2008; 80: 2222.
    • (2008) Analytical Chemistry , vol.80 , pp. 2222
    • Tong, X.1    Wren, J.C.2    Konermann, L.3
  • 200
    • 0033966669 scopus 로고    scopus 로고
    • OH radicals and oxidizing products in the gamma radiolysis of water
    • LaVerne JA. OH radicals and oxidizing products in the gamma radiolysis of water. Radiation Research 2000; 153: 196.
    • (2000) Radiation Research , vol.153 , pp. 196
    • LaVerne, J.A.1
  • 201
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • Barrick D, Baldwin RL. Three-state analysis of sperm whale apomyoglobin folding. Biochemistry 1993; 32: 3790.
    • (1993) Biochemistry , vol.32 , pp. 3790
    • Barrick, D.1    Baldwin, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.