메뉴 건너뛰기




Volumn 42, Issue 12, 2007, Pages 1569-1582

De novo sequencing of a 21-kDa cytochrome c4 from Thiocapsa roseopersicina by nanoelectrospray ionization ion-trap and Fourier-transform ion-cyclotron resonance mass spectrometry

Author keywords

Bottom up; Collision induced dissociation; Cytochrome c4; De novo protein sequencing; Electron capture dissociation; Electrospray ionization; Fourier transform ion cyclotron resonance; Ion trap; Liquid chromatography mass spectrometry

Indexed keywords

BOTTOM UP; COLLISION-INDUCED DISSOCIATION; DE NOVO PROTEIN SEQUENCING; ELECTRON-CAPTURE DISSOCIATION; FOURIER-TRANSFORM ION-CYCLOTRON RESONANCE; ION TRAP;

EID: 38149119842     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.1337     Document Type: Conference Paper
Times cited : (8)

References (40)
  • 1
    • 0024474304 scopus 로고
    • The role of cytochrome c4 in bacterial respiration. Cellular location and selective removal from membranes
    • Hunter DJB, Brown KR, Pettigrew GW. The role of cytochrome c4 in bacterial respiration. Cellular location and selective removal from membranes. Biochemical Journal 1989; 262: 233.
    • (1989) Biochemical Journal , vol.262 , pp. 233
    • Hunter, D.J.B.1    Brown, K.R.2    Pettigrew, G.W.3
  • 6
    • 0141884306 scopus 로고    scopus 로고
    • Peptide and protein de novo sequencing by mass spectrometry
    • Standing KG. Peptide and protein de novo sequencing by mass spectrometry. Current Opinion in Structural Biology 2003; 13: 595.
    • (2003) Current Opinion in Structural Biology , vol.13 , pp. 595
    • Standing, K.G.1
  • 8
    • 0001433809 scopus 로고
    • Method for determination of the amino acid sequence in peptides
    • Edman P. Method for determination of the amino acid sequence in peptides. Acta Chemica Scandinavica 1950; 4: 283.
    • (1950) Acta Chemica Scandinavica , vol.4 , pp. 283
    • Edman, P.1
  • 10
    • 0023143159 scopus 로고
    • The primary structure of Thioredoxin from Chromatium vinosum determined by high-performance tandem mass spectrometry
    • Johnson RS, Biemann K. The primary structure of Thioredoxin from Chromatium vinosum determined by high-performance tandem mass spectrometry. Biochemistry 1987; 26: 1209.
    • (1987) Biochemistry , vol.26 , pp. 1209
    • Johnson, R.S.1    Biemann, K.2
  • 11
    • 84994921866 scopus 로고
    • Mass spectrometric determination of the amino acid sequence of peptides and proteins
    • Biemann K, Martin SA. Mass spectrometric determination of the amino acid sequence of peptides and proteins. Mass Spectrometry Reviews 1987; 6: 1.
    • (1987) Mass Spectrometry Reviews , vol.6 , pp. 1
    • Biemann, K.1    Martin, S.A.2
  • 12
    • 0023645003 scopus 로고
    • Mass spectrometrically derived amino acid sequence of thioredoxin from Chlorobium, an evolutionarily prominent photosynthetic bacterium
    • Mathews WR, Johnson RS, Cornwell KL, Johnson TC, Buchanan BB, Biemann K. Mass spectrometrically derived amino acid sequence of thioredoxin from Chlorobium, an evolutionarily prominent photosynthetic bacterium. Journal of Biological Chemistry 1987; 262: 7537.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 7537
    • Mathews, W.R.1    Johnson, R.S.2    Cornwell, K.L.3    Johnson, T.C.4    Buchanan, B.B.5    Biemann, K.6
  • 13
    • 0024326913 scopus 로고
    • Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry
    • Hopper S, Johnson RS, Vath JE, Biemann K. Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry. Journal of Biological Chemistry 1989; 264: 20438.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 20438
    • Hopper, S.1    Johnson, R.S.2    Vath, J.E.3    Biemann, K.4
  • 14
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989; 246: 64.
    • (1989) Science , vol.246 , pp. 64
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 15
    • 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
  • 16
    • 33645813378 scopus 로고    scopus 로고
    • Review - Mass spectrometry and protein analysis
    • Domon B, Aebersold R. Review - Mass spectrometry and protein analysis. Science 2006; 312: 212.
    • (2006) Science , vol.312 , pp. 212
    • Domon, B.1    Aebersold, R.2
  • 17
  • 22
    • 24644470532 scopus 로고    scopus 로고
    • De novo sequencing sequencing of Atlantic cod vitellogenin tryptic peptides by matrix assisted laser desorption/ionization quadrupple time-of-flight tandem mass spectrometry: Similarities with haddock vitellogenin
    • Cohen AM, Mansour AAH, Banoub JH. De novo sequencing sequencing of Atlantic cod vitellogenin tryptic peptides by matrix assisted laser desorption/ionization quadrupple time-of-flight tandem mass spectrometry: similarities with haddock vitellogenin. Rapid Communications in Mass Spectrometry 2005; 19: 2454.
    • (2005) Rapid Communications in Mass Spectrometry , vol.19 , pp. 2454
    • Cohen, A.M.1    Mansour, A.A.H.2    Banoub, J.H.3
  • 23
    • 0015598626 scopus 로고
    • The amino acid sequences of cytochromes c-551 from three species of Pseudomonas
    • Ambler RP, Wynn M. The amino acid sequences of cytochromes c-551 from three species of Pseudomonas. Biochemical Journal 1973; 131: 485.
    • (1973) Biochemical Journal , vol.131 , pp. 485
    • Ambler, R.P.1    Wynn, M.2
  • 26
    • 0027461675 scopus 로고
    • Tandem mass spectrometry of very large molecules. 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization
    • Loo JA, Edmonds CG, Smith RD. Tandem mass spectrometry of very large molecules. 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization. Analytical Chemistry 1993; 65: 425.
    • (1993) Analytical Chemistry , vol.65 , pp. 425
    • Loo, J.A.1    Edmonds, C.G.2    Smith, R.D.3
  • 28
    • 0037353846 scopus 로고    scopus 로고
    • Statistical characterization of ion trap tandem mass spectra from doubly charged tryptic peptides
    • Tabb DL, Smith LL, Breci LA, Wysocki VH, Lin D, Yates JR. Statistical characterization of ion trap tandem mass spectra from doubly charged tryptic peptides. Analytical Chemistry 2003; 75: 1155.
    • (2003) Analytical Chemistry , vol.75 , pp. 1155
    • Tabb, D.L.1    Smith, L.L.2    Breci, L.A.3    Wysocki, V.H.4    Lin, D.5    Yates, J.R.6
  • 29
    • 0025984862 scopus 로고
    • Fragmentation of proteins by S. aureus strain V8 protease : Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acid
    • Sorensen SB, Sorensen TL, Breddam K. Fragmentation of proteins by S. aureus strain V8 protease : ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acid. FEBS Letters 1991; 294: 195.
    • (1991) FEBS Letters , vol.294 , pp. 195
    • Sorensen, S.B.1    Sorensen, T.L.2    Breddam, K.3
  • 34
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides
    • Geiger T, Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. The Journal of Biological Chemistry 1987; 262: 785.
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 785
    • Geiger, T.1    Clarke, S.2
  • 36
    • 33947366469 scopus 로고    scopus 로고
    • Side-chain losses in electron capture dissociation to improve peptide identification
    • Savitski MM, Nielsen ML, Zubarev RA. Side-chain losses in electron capture dissociation to improve peptide identification. Analytical Chemistry 2007; 79: 2296.
    • (2007) Analytical Chemistry , vol.79 , pp. 2296
    • Savitski, M.M.1    Nielsen, M.L.2    Zubarev, R.A.3
  • 38
    • 0025894050 scopus 로고
    • Primary structure diversity of prokaryotic diheme cytochromes c
    • Beeumen JV. Primary structure diversity of prokaryotic diheme cytochromes c. Biochimica et Biophysica Acta 1991; 1058: 56.
    • (1991) Biochimica et Biophysica Acta , vol.1058 , pp. 56
    • Beeumen, J.V.1
  • 40
    • 0035527414 scopus 로고    scopus 로고
    • Environmental diversity of bacteria and archaea
    • DeLong EF, Pace NR. Environmental diversity of bacteria and archaea. Systematic Biology 2001; 50: 470.
    • (2001) Systematic Biology , vol.50 , pp. 470
    • DeLong, E.F.1    Pace, N.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.