메뉴 건너뛰기




Volumn 22, Issue 2, 2011, Pages 300-309

Ion mobility-mass spectrometry study of folded ubiquitin conformers induced by treatment with cis-[Pd(en)(H 2O) 2] 2+

Author keywords

Ion mobility; Mass spectrometry; Pd(II) complexes; Proteomic reagents; Ubiquitin conformers

Indexed keywords

ACTIVATED COMPLEX; CHARGE STATE; ETHYLENE DIAMINE; ION MOBILITY; ION MOBILITY-MASS SPECTROMETRY; MOLAR EXCESS; PALLADIUM COMPLEXES; PD(II) COMPLEXES; PEPTIDE BONDS; PROTEOMIC REAGENTS; UBIQUITIN; UBIQUITIN CONFORMERS;

EID: 79952531652     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-010-0044-1     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 79952525238 scopus 로고    scopus 로고
    • Protein misfolding diseases
    • Bellotti, V., Stoppini, M.: Protein misfolding diseases. Open. Biol. J. 2, 228-234 (2009)
    • (2009) Open. Biol. J. , vol.2 , pp. 228-234
    • Bellotti, V.1    Stoppini, M.2
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M.: Protein folding and misfolding. Nature 426, 884-890 (2003)
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 7
    • 36348991325 scopus 로고    scopus 로고
    • Monitoring co-populated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry
    • Smith, D.P., Giles, K., Bateman, R.H., Radford, S.E., Ashcroft, A.E.: Monitoring co-populated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry. J. Am. Soc. Mass Spectrom. 18, 2180-2190 (2007)
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 2180-2190
    • Smith, D.P.1    Giles, K.2    Bateman, R.H.3    Radford, S.E.4    Ashcroft, A.E.5
  • 8
    • 60649094510 scopus 로고    scopus 로고
    • Collisional activation of protein complexes: Picking up the pieces
    • Benesch, J.L.P.: Collisional activation of protein complexes: picking up the pieces. J. Am. Soc. Mass Spectrom. 20, 341-348 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 341-348
    • Benesch, J.L.P.1
  • 9
    • 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
  • 11
    • 58149182318 scopus 로고    scopus 로고
    • Traveling wave ion mobility mass spectrometry studies of protein structure: Biological significance and comparison with x-ray crystallography and nuclear magnetic resonance spectroscopy measurements
    • Scarff, C.A., Thalassinos, K., Hilton, I., Scrivens, J.H.: Traveling wave ion mobility mass spectrometry studies of protein structure: biological significance and comparison with x-ray crystallography and nuclear magnetic resonance spectroscopy measurements. Rapid Commun. Mass Spectrom. 22, 3297-3304 (2008)
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 3297-3304
    • Scarff, C.A.1    Thalassinos, K.2    Hilton, I.3    Scrivens, J.H.4
  • 12
    • 58149477901 scopus 로고    scopus 로고
    • Characterization of phosphorylated peptides using traveling wave-based and drift cell ion mobility mass spectrometry
    • Thalassinos, K., Grabenauer, M., Slade, S.E., Hilton, G.R., Bowers, M. T., Scrivens, J.H.: Characterization of phosphorylated peptides using traveling wave-based and drift cell ion mobility mass spectrometry. Anal. Chem. 81, 248-254 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 248-254
    • Thalassinos, K.1    Grabenauer, M.2    Slade, S.E.3    Hilton, G.R.4    Bowers, M.T.5    Scrivens, J.H.6
  • 14
    • 71949092837 scopus 로고    scopus 로고
    • Use of ion mobility mass spectrometry and a collision cross-section algorithm to study an organometallic ruthenium anticancer complex and its adducts with a DNA oligonucleotide
    • Williams, J.P., Lough, J.A., Campuzano, I., Richardson, K., Sadler, P. J.: Use of ion mobility mass spectrometry and a collision cross-section algorithm to study an organometallic ruthenium anticancer complex and its adducts with a DNA oligonucleotide. Rapid Commun. Mass Spectrom. 23, 3563-3569 (2009)
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 3563-3569
    • Williams, J.P.1    Lough, J.A.2    Campuzano, I.3    Richardson, K.4    Sadler, P.J.5
  • 15
    • 0036569574 scopus 로고    scopus 로고
    • Palladium(II) complexes, as synthetic peptidases, regioselectively cleave the second peptide bond "upstream" from methionine and histidine side chains
    • Milović, N.M., Kostić, N.M.: Palladium(II) complexes, as synthetic peptidases, regioselectively cleave the second peptide bond "upstream" from methionine and histidine side chains. J. Am. Chem. Soc. 124, 4759-4769 (2002)
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4759-4769
    • Milović, N.M.1    Kostić, N.M.2
  • 16
    • 0037460193 scopus 로고    scopus 로고
    • Palladium(II) complex as a sequence-specific peptidase: Hydrolytic cleavage under mild conditions of x-pro peptide bonds in x-pro-met and x-pro-his segments
    • Milović, N.M., Kostić, N.M.: Palladium(II) complex as a sequence-specific peptidase: hydrolytic cleavage under mild conditions of x-pro peptide bonds in x-pro-met and x-pro-his segments. J. Am. Chem. Soc. 125, 781-788 (2003)
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 781-788
    • Milović, N.M.1    Kostić, N.M.2
  • 17
    • 64649107204 scopus 로고    scopus 로고
    • Metal-coded affinity tag labeling: A demonstration of analytical robustness and suitability for biological applications
    • Ahrends, R., Pieper, S., Neumann, B., Scheler, C., Linscheld, M.W.: Metal-coded affinity tag labeling: a demonstration of analytical robustness and suitability for biological applications. Anal. Chem. 81, 2176-2184 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 2176-2184
    • Ahrends, R.1    Pieper, S.2    Neumann, B.3    Scheler, C.4    Linscheld, M.W.5
  • 18
    • 0037112137 scopus 로고    scopus 로고
    • Sequence-dependent cleavage of albumins with palladium(II) complexes: Role of serine residue in controlling the high regioselectivity of protein cleavage
    • Zhu, L., Kostić, N.M.: Sequence-dependent cleavage of albumins with palladium(II) complexes: role of serine residue in controlling the high regioselectivity of protein cleavage. Inorg. Chim. Acta 339, 104-110 (2002)
    • (2002) Inorg. Chim. Acta , vol.339 , pp. 104-110
    • Zhu, L.1    Kostić, N.M.2
  • 19
    • 0031875161 scopus 로고    scopus 로고
    • Transition-metal complexes as alternatives to proteolytic enzymes. regioselective cleavage of myoglobin by palladium(II) aqua complexes
    • hu, L., Bakhtiar, R., Kostić, N.M.: Transition-metal complexes as alternatives to proteolytic enzymes. regioselective cleavage of myoglobin by palladium(II) aqua complexes. J. Biol. Inorg. Chem. 3, 383-391 (1998)
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 383-391
    • Hu, L.1    Bakhtiar, R.2    Kostić, N.M.3
  • 20
    • 0037203125 scopus 로고    scopus 로고
    • Interplay of terminal amino group and coordinating side chains in directing regioselective cleavage of natural peptides and proteins with palladium(II) complexes
    • Milović, N.M., Kostić, N.M.: Interplay of terminal amino group and coordinating side chains in directing regioselective cleavage of natural peptides and proteins with palladium(II) complexes. Inorg. Chem. 41, 7053-7063 (2002)
    • (2002) Inorg. Chem. , vol.41 , pp. 7053-7063
    • Milović, N.M.1    Kostić, N.M.2
  • 22
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar, S., Bugg, C.E., Cook, W.J.: Structure of ubiquitin refined at 1.8 Å resolution. J. Mol. Biol. 194, 531-544 (1987)
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 23
    • 56749155588 scopus 로고    scopus 로고
    • Structural probing of Zn(II), Cd(II), and Hg(II) binding to human ubiquitin
    • Falini, G., Fermani, S., Tosi, G., Arnesano, F., Natile, G.: Structural probing of Zn(II), Cd(II), and Hg(II) binding to human ubiquitin. Chem. Commun. 45, 5960-5962 (2008)
    • (2008) Chem. Commun. , vol.45 , pp. 5960-5962
    • Falini, G.1    Fermani, S.2    Tosi, G.3    Arnesano, F.4    Natile, G.5
  • 26
    • 84864164550 scopus 로고    scopus 로고
    • Clemmer, D. E. http://www.indiana.edu/~clemmer/Research/research.htm
    • Clemmer, D.E.1
  • 27
    • 33846444321 scopus 로고    scopus 로고
    • Resolution and structural transitions of elongated states of ubiquitin
    • Koeniger, S.L., Clemmer, D.E.: Resolution and structural transitions of elongated states of ubiquitin. J. Am. Soc.Mass Spectrom. 18, 322-331 (2007)
    • (2007) J. Am. Soc.Mass Spectrom. , vol.18 , pp. 322-331
    • Koeniger, S.L.1    Clemmer, D.E.2
  • 28
    • 33646357505 scopus 로고    scopus 로고
    • Evidence for many resolvable structures within conformational types of electrosprayed ubiquitin ions
    • Koeniger, S.L., Merenbloom, S.I., Clemmer, D.E.: Evidence for many resolvable structures within conformational types of electrosprayed ubiquitin ions. J. Phys. Chem. B 110, 7017-7021 (2006)
    • (2006) J. Phys. Chem. B , vol.110 , pp. 7017-7021
    • Koeniger, S.L.1    Merenbloom, S.I.2    Clemmer, D.E.3
  • 29
    • 33748338997 scopus 로고    scopus 로고
    • Transfer of structural elements from compact to extended states in unsolvated ubiquitin
    • Koeniger, S.L., Merenbloom, S.I., Sundarapandian, S., Clemmer, D.E.: Transfer of structural elements from compact to extended states in unsolvated ubiquitin. J. Am. Chem. Soc. 128, 11713-11719 (2006)
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11713-11719
    • Koeniger, S.L.1    Merenbloom, S.I.2    Sundarapandian, S.3    Clemmer, D.E.4
  • 30
    • 0034480635 scopus 로고    scopus 로고
    • Investigation of bovine ubiquitin conformers separated by high-field asymmetric waveform ion mobility spectrometry: Cross section measurements using energy-loss experiments with a triple quadrupole mass spectrometer
    • Purves, R.W., Barnett, D.A., Ells, B., Guevremont, R.: Investigation of bovine ubiquitin conformers separated by high-field asymmetric waveform ion mobility spectrometry: cross section measurements using energy-loss experiments with a triple quadrupole mass spectrometer. J. Am. Soc. Mass Spectrom. 11, 738-745 (2000)
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 738-745
    • Purves, R.W.1    Barnett, D.A.2    Ells, B.3    Guevremont, R.4
  • 31
    • 33748966336 scopus 로고    scopus 로고
    • The role of conformation on electron capture dissociation of ubiquitin
    • Robinson, E.W., Leib, R.D., Williams, E.R.: The role of conformation on electron capture dissociation of ubiquitin. J. Am. Soc. Mass Spectrom. 17, 1469-1479 (2006)
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1469-1479
    • Robinson, E.W.1    Leib, R.D.2    Williams, E.R.3
  • 32
    • 33748362649 scopus 로고    scopus 로고
    • Mass spectrometry assisted assignments of binding and cleavage sites of copper(II) and platinum(II) complexes towards oxidized insulin B chain
    • Hong, J., Miao, R., Zhao, C., Jiang, J., Tang, H., Zhu, L.: Mass spectrometry assisted assignments of binding and cleavage sites of copper(II) and platinum(II) complexes towards oxidized insulin B chain. J. Mass Spectrom. 41, 1061-1072 (2006)
    • (2006) J. Mass Spectrom. , vol.41 , pp. 1061-1072
    • Hong, J.1    Miao, R.2    Zhao, C.3    Jiang, J.4    Tang, H.5    Zhu, L.6
  • 33
    • 33947455648 scopus 로고
    • The stereochemistry of complex inorganic compounds. X. The stereoisomers of dichlorobis(ethylenediamine) platinum(IV) chloride
    • Basolo, F., Bailar Jr., J.C., Tarr, B.R.: The stereochemistry of complex inorganic compounds. X. The stereoisomers of dichlorobis(ethylenediamine) platinum(IV) chloride. J. Am. Chem. Soc. 72, 2433-2438 (1950)
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 2433-2438
    • Basolo, F.1    Bailar Jr., J.C.2    Tarr, B.R.3
  • 34
    • 0000101035 scopus 로고
    • The stereoisomerism of complex inorganic compounds. XVI. The stereoisomers of dichlorobis(ethylenediamine) platinum(IV) salts
    • Heneghan, L.F., Bailar Jr., J.C.: The stereoisomerism of complex inorganic compounds. XVI. The stereoisomers of dichlorobis(ethylenediamine) platinum(IV) salts. J. Am. Chem. Soc. 75, 1840-1841 (1953)
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 1840-1841
    • Heneghan, L.F.1    Bailar Jr., J.C.2
  • 35
    • 0001609919 scopus 로고
    • Ammine ligand exchange in tetra-amminepalladium(II) in aqueous solution
    • Broennum, B., Johansen, H.S., Skibsted, L.H.: Ammine ligand exchange in tetra-amminepalladium(II) in aqueous solution. Acta Chem. Scand. 43, 975-980 (1989)
    • (1989) Acta Chem. Scand. , vol.43 , pp. 975-980
    • Broennum, B.1    Johansen, H.S.2    Skibsted, L.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.