메뉴 건너뛰기




Volumn 23, Issue 11, 2012, Pages 1911-1920

Ligand migration in the gaseous insulin-CB7 Complex - A cautionary tale about the use of ECD-MS for ligand binding site determination

Author keywords

Cucurbituril; Electron capture dissociation; Fourier transform ion cyclotron resonance mass spectrometry; Insulin; Ion activation; Ligand binding site determination

Indexed keywords

CUCURBITURILS; ELECTRON CAPTURE DISSOCIATION; FOURIER-TRANSFORM ION CYCLOTRON RESONANCE MASS SPECTROMETRY; ION ACTIVATION; LIGAND-BINDING SITES;

EID: 84868242023     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-012-0470-3     Document Type: Article
Times cited : (14)

References (43)
  • 1
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J.: Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16, 1-23 (1997)
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1-23
    • Loo, J.1
  • 2
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck, A.J.R., van den Heuvel, R.H.H.: Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 23, 368-389 (2004)
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 368-389
    • Heck, A.J.R.1    Van Den Heuvel, R.H.H.2
  • 3
    • 34249947523 scopus 로고    scopus 로고
    • Intermolecular interactions in biomolecular systems examined by mass spectrometry
    • Wyttenbach, T., Bowers, M.T.: Intermolecular interactions in biomolecular systems examined by mass spectrometry. Annu. Rev. Phys. Chem. 58, 511-533 (2007)
    • (2007) Annu. Rev. Phys. Chem. , vol.58 , pp. 511-533
    • Wyttenbach, T.1    Bowers, M.T.2
  • 4
    • 9744245284 scopus 로고    scopus 로고
    • The study of protein-ligand interactions by mass spectrometry - A personal view
    • Breuker, K.: The study of protein-ligand interactions by mass spectrometry - a personal view. Int. J. Mass Spectrom. 239, 33-41 (2004)
    • (2004) Int. J. Mass Spectrom. , vol.239 , pp. 33-41
    • Breuker, K.1
  • 7
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • Hernández, H., Robinson, C.V.: Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat. Protoc. 2, 715-726 (2007)
    • (2007) Nat. Protoc. , vol.2 , pp. 715-726
    • Hernández, H.1    Robinson, C.V.2
  • 8
    • 77956181968 scopus 로고    scopus 로고
    • When proteomics meets structural biology
    • Zhou, M., Robinson, C.V.: When proteomics meets structural biology. Trends Biochem. Sci. 35, 522-529 (2010)
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 522-529
    • Zhou, M.1    Robinson, C.V.2
  • 9
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: A bridge between interactomics and structural biology
    • Heck, A.J.R.: Native mass spectrometry: a bridge between interactomics and structural biology. Nat. Methods 5, 927-933 (2008)
    • (2008) Nat. Methods , vol.5 , pp. 927-933
    • Heck, A.J.R.1
  • 10
    • 0037236038 scopus 로고    scopus 로고
    • A top down approach to protein structural studies using chemical cross-linking and fourier transform mass spectrometry
    • Kruppa, G.H., Schoeniger, J., Young, M.M.: A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry. Rapid Commun. Mass Spectrom. 17, 155-162 (2003)
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 155-162
    • Kruppa, G.H.1    Schoeniger, J.2    Young, M.M.3
  • 12
    • 25144445202 scopus 로고    scopus 로고
    • Structural proteomics of macromolecular assemblies using oxidative footprinting and mass spectrometry
    • Guan, J.-Q., Chance, M.R.: Structural proteomics of macromolecular assemblies using oxidative footprinting and mass spectrometry. Trends Biochem. Sci. 30, 583-592 (2005)
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 583-592
    • Guan, J.-Q.1    Chance, M.R.2
  • 13
    • 80052989416 scopus 로고    scopus 로고
    • Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4
    • Gau, B., Garai, K., Frieden, C., Gross, M.L.: Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4. Biochemistry 50, 8117-8126 (2011)
    • (2011) Biochemistry , vol.50 , pp. 8117-8126
    • Gau, B.1    Garai, K.2    Frieden, C.3    Gross, M.L.4
  • 14
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • Zubarev, R.A., Kelleher, N.L., McLafferty, F.W.: Electron capture dissociation of multiply charged protein cations. A nonergodic process. J. Am. Chem. Soc. 120, 3265-3266 (1998)
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 15
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka, J.E.P., Coon, J.J., Schroeder, M.J., Shabanowitz, J., Hunt, D.F.: Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 101, 9528-9533 (2004)
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9528-9533
    • Syka, J.E.P.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 16
    • 14344257790 scopus 로고    scopus 로고
    • Detection and localization of protein modifications by high resolution tandem mass spectrometry
    • Meng, F., Forbes, A.J., Miller, L.M., Kelleher, N.L.: Detection and localization of protein modifications by high resolution tandem mass spectrometry. Mass Spectrom. Rev. 24, 126-134 (2005)
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 126-134
    • Meng, F.1    Forbes, A.J.2    Miller, L.M.3    Kelleher, N.L.4
  • 17
    • 35848949043 scopus 로고    scopus 로고
    • Decoding protein modifications using top-down mass spectrometry
    • Siuti, N., Kelleher, N.L.: Decoding protein modifications using top-down mass spectrometry. Nat. Methods 4, 817-821 (2007)
    • (2007) Nat. Methods , vol.4 , pp. 817-821
    • Siuti, N.1    Kelleher, N.L.2
  • 19
    • 0037133237 scopus 로고    scopus 로고
    • Top-down mass spectrometry of a 29-kDa protein for characterization of any posttranslational modification to within one residue
    • Sze, S.K., Ge, Y., Oh, H., McLafferty, F.W.: Top-down mass spectrometry of a 29-kDa protein for characterization of any posttranslational modification to within one residue. Proc. Natl. Acad. Sci. U.S.A. 99, 1774-1779 (2002)
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1774-1779
    • Sze, S.K.1    Ge, Y.2    Oh, H.3    McLafferty, F.W.4
  • 22
    • 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, J.A.: Top-down ESI-ECD-FT-ICR mass spectrometry localizes noncovalent protein-ligand binding sites. J. Am. Chem. Soc. 128, 14432-14433 (2006)
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14432-14433
    • Xie, Y.1    Zhang, J.2    Yin, S.3    Loo, J.A.4
  • 23
    • 77952886478 scopus 로고    scopus 로고
    • Elucidating the site of protein-ATP binding by top-down mass spectrometry
    • Yin, S., Loo, J.A.: Elucidating the site of protein-ATP binding by top-down mass spectrometry. J. Am. Soc. Mass Spectrom. 21, 899-907 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 899-907
    • Yin, S.1    Loo, J.A.2
  • 24
    • 77958100537 scopus 로고    scopus 로고
    • Top-down mass spectrometry of supercharged native protein-ligand complexes
    • Yin, S., Loo, J.A.: Top-down mass spectrometry of supercharged native protein-ligand complexes. Int. J. Mass Spectrom. 300, 118-122 (2011)
    • (2011) Int. J. Mass Spectrom. , vol.300 , pp. 118-122
    • Yin, S.1    Loo, J.A.2
  • 25
    • 79960370853 scopus 로고    scopus 로고
    • Native electrospray and electron-capture dissociation FTICR mass spectrometry for top-down studies of protein assemblies
    • Zhang, H., Cui, W., Wen, J., Blankenship, R.E., Gross, M.L.: Native electrospray and electron-capture dissociation FTICR mass spectrometry for top-down studies of protein assemblies. Anal. Chem. 83, 5598-5606 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 5598-5606
    • Zhang, H.1    Cui, W.2    Wen, J.3    Blankenship, R.E.4    Gross, M.L.5
  • 26
    • 80052542626 scopus 로고    scopus 로고
    • Mapping a noncovalent protein-peptide interface by top-down FTICR mass spectrometry using electron capture dissociation
    • Clarke, D.J., Murray, E., Hupp, T., Mackay, C.L., Langridge-Smith, P.R.R.: Mapping a noncovalent protein-peptide interface by top-down FTICR mass spectrometry using electron capture dissociation. J. Am. Soc. Mass Spectrom. 22, 1432-1440 (2011)
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1432-1440
    • Clarke, D.J.1    Murray, E.2    Hupp, T.3    Mackay, C.L.4    Langridge-Smith, P.R.R.5
  • 30
  • 32
    • 0000743715 scopus 로고
    • Structure and selectivity in host-guest complexes of cucurbituril
    • Mock, W.L., Shih, N.-Y.: Structure and selectivity in host-guest complexes of cucurbituril. J. Org. Chem. 51, 4440-4446 (1986)
    • (1986) J. Org. Chem. , vol.51 , pp. 4440-4446
    • Mock, W.L.1    Shih, N.-Y.2
  • 33
    • 0000821871 scopus 로고
    • Organic ligand-receptor interactions between cucurbituril and alkylammonium ions
    • Mock, W.L., Shih, N.-Y.: Organic ligand-receptor interactions between cucurbituril and alkylammonium ions. J. Am. Chem. Soc. 110, 4706-4710 (1988)
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 4706-4710
    • Mock, W.L.1    Shih, N.-Y.2
  • 34
    • 0033624860 scopus 로고    scopus 로고
    • Enhancing the T-9R transition of insulin by helix-promoting sequence modifications at the N-terminal B-chain
    • Shneine, J., Voswinkel, M., Federwisch, M., Wollmer, A.: Enhancing the T-9R transition of insulin by helix-promoting sequence modifications at the N-terminal B-chain. Biol. Chem. 381, 127-133 (2000)
    • (2000) Biol. Chem. , vol.381 , pp. 127-133
    • Shneine, J.1    Voswinkel, M.2    Federwisch, M.3    Wollmer, A.4
  • 35
    • 0025778802 scopus 로고
    • Comparative 2D NMR studies of human insulin and despentapeptide insulin: Sequential resonance assignment and implications for protein dynamics and receptor recognition
    • Hua, Q., Weiss, M.A.: Comparative 2D NMR studies of human insulin and despentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition. Biochemistry 30, 5505-5515 (1991)
    • (1991) Biochemistry , vol.30 , pp. 5505-5515
    • Hua, Q.1    Weiss, M.A.2
  • 36
    • 0033620364 scopus 로고    scopus 로고
    • Electron capture dissociation of gaseous multiply-charged proteins is favored at disulfide bonds and other sites of high hydrogen atom affinity
    • Zubarev, R.A., Kruger, N.A., Fridriksson, E.K., Lewis, M.A., Horn, D.M., Carpenter, B.K., McLafferty, F.W.: Electron capture dissociation of gaseous multiply-charged proteins is favored at disulfide bonds and other sites of high hydrogen atom affinity. J. Am. Chem. Soc. 121, 2857-2862 (1999)
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2857-2862
    • Zubarev, R.A.1    Kruger, N.A.2    Fridriksson, E.K.3    Lewis, M.A.4    Horn, D.M.5    Carpenter, B.K.6    McLafferty, F.W.7
  • 37
    • 34547629235 scopus 로고    scopus 로고
    • Label-free continuous enzyme assays with macrocycle-fluorescent dye complexes
    • Hennig, A., Bakirci, H., Nau, W.M.: Label-free continuous enzyme assays with macrocycle-fluorescent dye complexes. Nat. Methods 4, 629-632 (2007)
    • (2007) Nat. Methods , vol.4 , pp. 629-632
    • Hennig, A.1    Bakirci, H.2    Nau, W.M.3
  • 38
    • 53849103262 scopus 로고    scopus 로고
    • Supramolecular tandem enzyme assays for multiparameter sensor arrays and enantiomeric excess determination of amino acids
    • Bailey, D.M., Hennig, A., Uzunova, V.D., Nau, W.M.: Supramolecular tandem enzyme assays for multiparameter sensor arrays and enantiomeric excess determination of amino acids. Chem. Eur. J. 14, 6069-6077 (2008)
    • (2008) Chem. Eur. J. , vol.14 , pp. 6069-6077
    • Bailey, D.M.1    Hennig, A.2    Uzunova, V.D.3    Nau, W.M.4
  • 39
    • 70349108740 scopus 로고    scopus 로고
    • Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: The effect of ligand binding on conformational stability
    • Hopper, J.T.S., Oldham, N.J.: Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: the effect of ligand binding on conformational stability. J. Am. Soc. Mass Spectrom. 20, 1851-1858 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1851-1858
    • Hopper, J.T.S.1    Oldham, N.J.2
  • 41
    • 63849305221 scopus 로고    scopus 로고
    • Supramolecular modification of ion chemistry: Modulation of peptide charge state and dissociation behavior through complexation with cucurbituril (n 0 5, 6) or alpha-cyclodextrin
    • Zhang, H., Grabenauer, M., Bowers, M.T., Dearden, D.V.: Supramolecular Modification of Ion Chemistry: Modulation of Peptide Charge State and Dissociation Behavior through Complexation with cucurbituril (n 0 5, 6) or alpha-Cyclodextrin. J. Phys. Chem. A 113, 1508-1517 (2009)
    • (2009) J. Phys. Chem. A , vol.113 , pp. 1508-1517
    • Zhang, H.1    Grabenauer, M.2    Bowers, M.T.3    Dearden, D.V.4
  • 42
    • 80054684751 scopus 로고    scopus 로고
    • Host-guest chemistry in the gas phase: Selected fragmentations of CB[6]-peptide complexes at lysine residues and its utility to probe the structures of small proteins
    • Heo, S.W., Choi, T.S., Park, K.M., Ko, Y.H., Kim, S.B., Kim, K., Kim, H.I.: Host-Guest Chemistry in the Gas Phase: Selected Fragmentations of CB[6]-Peptide Complexes at Lysine Residues and Its Utility to Probe the Structures of Small Proteins. Anal. Chem. 83, 7916-7923 (2011)
    • (2011) Anal. Chem. , vol.83 , pp. 7916-7923
    • Heo, S.W.1    Choi, T.S.2    Park, K.M.3    Ko, Y.H.4    Kim, S.B.5    Kim, K.6    Kim, H.I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.