메뉴 건너뛰기




Volumn 25, Issue 14, 2011, Pages 1949-1958

Characterization of Nα-Fmoc-protected dipeptide isomers by electrospray ionization tandem mass spectrometry (ESI-MSn): Effect of protecting group on fragmentation of dipeptides

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROSPRAY IONIZATION; ISOMERS; MASS SPECTROMETRY; NEGATIVE IONS; PROTONATION; SPECTRUM ANALYZERS;

EID: 79959636685     PISSN: 09514198     EISSN: 10970231     Source Type: Journal    
DOI: 10.1002/rcm.5076     Document Type: Article
Times cited : (9)

References (53)
  • 1
    • 0007193238 scopus 로고    scopus 로고
    • Chemical synthesis of natural product peptides: Coupling methods for the incorporation of noncoded amino acids into peptides
    • J. M. Humphery, A. R. Chamberlin,. Chemical synthesis of natural product peptides: coupling methods for the incorporation of noncoded amino acids into peptides. Chem. Rev. 1997, 97, 2243.
    • (1997) Chem. Rev. , vol.97 , pp. 2243
    • Humphery, J.M.1    Chamberlin, A.R.2
  • 3
    • 0038215381 scopus 로고    scopus 로고
    • Identification of potent and broad-spectrum antibiotics from SAR studies of a synthetic vancomycin analogue
    • K. A. Ahrendt, J. A. Olesen, M. Wakao, J. Trias, J. A. Ellman,. Identification of potent and broad-spectrum antibiotics from SAR studies of a synthetic vancomycin analogue. Bio. Org. Med. Chem. Lett. 2003, 13, 1683.
    • (2003) Bio. Org. Med. Chem. Lett. , vol.13 , pp. 1683
    • Ahrendt, K.A.1    Olesen, J.A.2    Wakao, M.3    Trias, J.4    Ellman, J.A.5
  • 5
    • 2142752826 scopus 로고
    • The 9-fluorenylmethoxycarbonyl function, a new base-sensitive amino-protecting group
    • (a),.
    • (a), L. A. Carpino, G. Y. Han,. The 9-fluorenylmethoxycarbonyl function, a new base-sensitive amino-protecting group. J. Am. Chem. Soc. 1970, 92, 5748
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 5748
    • Carpino, L.A.1    Han, G.Y.2
  • 6
    • 0005215827 scopus 로고
    • The 9-fluorenylmethyloxycarbonyl family of base-sensitive amino-protecting groups
    • (b).
    • (b), L. A. Carpino,. The 9-fluorenylmethyloxycarbonyl family of base-sensitive amino-protecting groups. Acc. Chem. Res. 1987, 20, 401-407.
    • (1987) Acc. Chem. Res. , vol.20 , pp. 401-407
    • Carpino, L.A.1
  • 7
    • 21844457685 scopus 로고    scopus 로고
    • Fragmentation pathways of protonated peptides
    • references cited therein.
    • B. Paizs, S. Suhai,. Fragmentation pathways of protonated peptides. Mass Spectrom. Rev. 2005, 24, 508, and references cited therein.
    • (2005) Mass Spectrom. Rev. , vol.24 , pp. 508
    • Paizs, B.1    Suhai, S.2
  • 8
    • 0034082949 scopus 로고    scopus 로고
    • Reaction competition in the fragmentation of protonated dipeptides
    • A. G. Harrison, I. G. Csizmadia, T. H. Tang, Y. P. Tu,. Reaction competition in the fragmentation of protonated dipeptides. J. Mass Spectrom. 2000, 35, 683.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 683
    • Harrison, A.G.1    Csizmadia, I.G.2    Tang, T.H.3    Tu, Y.P.4
  • 9
    • 0035029537 scopus 로고    scopus 로고
    • Theoretical study of the main fragmentation pathways for protonated glycylglycine
    • B. Paizs, S. Suhai,. Theoretical study of the main fragmentation pathways for protonated glycylglycine. Rapid Commun. Mass Spectrom. 2001, 15, 651.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 651
    • Paizs, B.1    Suhai, S.2
  • 10
    • 84989051599 scopus 로고
    • Tandem mass spectrometry of peptides: Sequence information based on neutral losses. I. Isomeric dipeptides
    • M. M. Cordero, C. Wesdemiotis,. Tandem mass spectrometry of peptides: sequence information based on neutral losses. I. Isomeric dipeptides. Org. Mass Spectrom. 1993, 28, 1041.
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1041
    • Cordero, M.M.1    Wesdemiotis, C.2
  • 11
    • 84989039096 scopus 로고
    • Characterization of Z-blocked isomeric dipeptides by fast atom bombardment tandem mass spectrometry and kinetic energy release measurements
    • E. Mammoliti, G. Sindona, N. Uccella,. Characterization of Z-blocked isomeric dipeptides by fast atom bombardment tandem mass spectrometry and kinetic energy release measurements, Org. Mass Spectrom. 1992, 27, 495.
    • (1992) Org. Mass Spectrom. , vol.27 , pp. 495
    • Mammoliti, E.1    Sindona, G.2    Uccella, N.3
  • 12
    • 0034516862 scopus 로고    scopus 로고
    • Dissociation of the peptide bond in protonated peptides
    • M. J. Polce, D. Ren, C. Wesdemiotis,. Dissociation of the peptide bond in protonated peptides. J. Mass Spectrom. 2000, 35, 1391.
    • (2000) J. Mass Spectrom. , vol.35 , pp. 1391
    • Polce, M.J.1    Ren, D.2    Wesdemiotis, C.3
  • 13
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons
    • M. Karas, F. Hillenkamp,. Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons. Anal. Chem. 1988, 60, 2299
    • (1988) Anal. Chem. , vol.60 , pp. 2299
    • Karas, M.1    Hillenkamp, F.2
  • 14
    • 15444379533 scopus 로고
    • Detection of high mass molecular ions by laser desorption time-of-flight mass spectrometry (in Japanese)
    • (b),.
    • (b), T. Yoshida, K. Tanaka, Y. Ido, S. Akita, K. Yoshida,. Detection of high mass molecular ions by laser desorption time-of-flight mass spectrometry (in Japanese). Shitsuryo Bunseki Mass Spectrometry. 1988, 36, 59.
    • (1988) Shitsuryo Bunseki Mass Spectrometry. , vol.36 , pp. 59
    • Yoshida, T.1    Tanaka, K.2    Ido, Y.3    Akita, S.4    Yoshida, K.5
  • 15
    • 0037211939 scopus 로고    scopus 로고
    • A comparison of negative and positive ion time-of-flight post source-decay mass spectrometry for peptides containing basic residues
    • N. L. Clipston, J. Jai-nhuknan, C. J. Cassady,. A comparison of negative and positive ion time-of-flight post source-decay mass spectrometry for peptides containing basic residues. Int. J. Mass Spectrom. 2003, 222, 363.
    • (2003) Int. J. Mass Spectrom. , vol.222 , pp. 363
    • Clipston, N.L.1    Jai-Nhuknan, J.2    Cassady, C.J.3
  • 16
    • 34548014772 scopus 로고    scopus 로고
    • Proteins sequence information by matrix-assisted laser desorption ionization/time-of-flight mass spectrometry
    • J. Hardouin,. Proteins sequence information by matrix-assisted laser desorption ionization/time-of-flight mass spectrometry. Mass Spectrom. Rev. 2007, 26, 672.
    • (2007) Mass Spectrom. Rev. , vol.26 , pp. 672
    • Hardouin, J.1
  • 17
    • 2442558217 scopus 로고    scopus 로고
    • Isomeric discrimination of arginine-containing dipeptides using electrospray ionization ion trap mass spectrometry and the kinetic method
    • K. A. Schug, W. Linder, K. Lemr,. Isomeric discrimination of arginine-containing dipeptides using electrospray ionization ion trap mass spectrometry and the kinetic method. J. Am. Soc. Mass Spectrom. 2004, 15, 840.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 840
    • Schug, K.A.1    Linder, W.2    Lemr, K.3
  • 18
    • 15444367804 scopus 로고    scopus 로고
    • Characterization of dipeptide isomers by tandem mass spectrometry of their mono- versus dilithiated complexes
    • F. Pingitore, C. Wesdemiotis,. Characterization of dipeptide isomers by tandem mass spectrometry of their mono- versus dilithiated complexes. Anal. Chem. 2005, 77, 1796.
    • (2005) Anal. Chem. , vol.77 , pp. 1796
    • Pingitore, F.1    Wesdemiotis, C.2
  • 19
    • 0035566202 scopus 로고    scopus 로고
    • Differentiation and quantitation of isomeric dipeptides by low energy dissociation of copper(II)-bound complexes
    • W. Andy Tao, L. Wu, R. G. Cooks,. Differentiation and quantitation of isomeric dipeptides by low energy dissociation of copper(II)-bound complexes. J. Am. Soc. Mass Spectrom. 2001, 12, 490.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 490
    • Andy Tao, W.1    Wu, L.2    Cooks, R.G.3
  • 20
    • 35448957973 scopus 로고    scopus 로고
    • Fragmentation of protonated dipeptides containing arginine. Effect of activation method
    • M. W. Forbes, R. A. Jockusch, A. B. Young, A. G. Harrison,. Fragmentation of protonated dipeptides containing arginine. Effect of activation method. J. Am. Soc. Mass Spectrom. 2007, 18, 1959.
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1959
    • Forbes, M.W.1    Jockusch, R.A.2    Young, A.B.3    Harrison, A.G.4
  • 21
    • 0028799323 scopus 로고
    • Tandem mass spectrometry of peptides. III. Differentiation between leucine and isoleucine based on neutral losses
    • N. L. Squire, S. Beranova, C. Wesdemiotis,. Tandem mass spectrometry of peptides. III. Differentiation between leucine and isoleucine based on neutral losses. J. Mass Spectrom. 1995, 30, 1429.
    • (1995) J. Mass Spectrom. , vol.30 , pp. 1429
    • Squire, N.L.1    Beranova, S.2    Wesdemiotis, C.3
  • 22
    • 66249093162 scopus 로고    scopus 로고
    • Reactivity of Tyr-Leu and Leu-Tyr dipeptides: Identification of oxidation products by liquid chromatography-tandem mass spectrometry
    • C. Fonseca, M. R. M. Domingues, C. Simoes, F. Amado, P. Domingues,. Reactivity of Tyr-Leu and Leu-Tyr dipeptides: identification of oxidation products by liquid chromatography-tandem mass spectrometry. J. Mass Spectrom. 2009, 44, 681.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 681
    • Fonseca, C.1    Domingues, M.R.M.2    Simoes, C.3    Amado, F.4    Domingues, P.5
  • 23
    • 70349144105 scopus 로고    scopus 로고
    • Metastable atom-activated dissociation mass spectrometry: Leucine/isoleucine differentiation and ring cleavage of proline residues
    • S. L. Cook, O. L. Collin, G. P. Jackson,. Metastable atom-activated dissociation mass spectrometry: leucine/isoleucine differentiation and ring cleavage of proline residues. J. Mass Spectrom. 2009, 44, 1211.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 1211
    • Cook, S.L.1    Collin, O.L.2    Jackson, G.P.3
  • 24
    • 49149116456 scopus 로고    scopus 로고
    • 1-1 product ions in the mass spectra of N-{para-(ferrocenyl)benzoyl} dipeptide esters
    • 1-1 product ions in the mass spectra of N-{para-(ferrocenyl)benzoyl} dipeptide esters. Rapid Commun. Mass Spectrom. 2008, 22, 2398.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 2398
    • Goel, A.1    Kenny, P.T.M.2
  • 25
    • 0031026946 scopus 로고    scopus 로고
    • Pathways to immonium ions in the fragmentation of protonated peptides
    • K. Ambihapathy, T. Jalcin, H. W. Leung, A. G. Harrison,. Pathways to immonium ions in the fragmentation of protonated peptides. J. Mass Spectrom. 1997, 32, 209.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 209
    • Ambihapathy, K.1    Jalcin, T.2    Leung, H.W.3    Harrison, A.G.4
  • 27
    • 0037212299 scopus 로고    scopus 로고
    • Involvement of salt bridges in a novel gas phase rearrangement of protonated arginine-containing dipeptides which precedes fragmentation
    • J. M. Farrugia, R. A. J. O'Hair,. Involvement of salt bridges in a novel gas phase rearrangement of protonated arginine-containing dipeptides which precedes fragmentation. Int. J. Mass Spectrom. 2003, 222, 229
    • (2003) Int. J. Mass Spectrom. , vol.222 , pp. 229
    • Farrugia, J.M.1    O'Hair, R.A.J.2
  • 28
    • 0024081048 scopus 로고
    • The determination of the amino acid sequence in the fast atom bombardment mass spectra of dipeptides
    • W. Kulik, W. Heerma,. The determination of the amino acid sequence in the fast atom bombardment mass spectra of dipeptides. Biomed. Environ. Mass Spectrom. 1988, 17, 173.
    • (1988) Biomed. Environ. Mass Spectrom. , vol.17 , pp. 173
    • Kulik, W.1    Heerma, W.2
  • 29
    • 0024423506 scopus 로고
    • Fast atom bombardment tandem mass spectrometry for amino acid sequence determination in tripeptides
    • W. Kulik, W. Heerma,. Fast atom bombardment tandem mass spectrometry for amino acid sequence determination in tripeptides. Biol. Mass Spectrom. 1989, 18, 910.
    • (1989) Biol. Mass Spectrom. , vol.18 , pp. 910
    • Kulik, W.1    Heerma, W.2
  • 30
    • 0025063727 scopus 로고
    • Isomeric tripeptides: A study on structure-spectrum relationship
    • D. Von Setten, W. Kulik, W. Heerma,. Isomeric tripeptides: a study on structure-spectrum relationship. Biomed. Environ. Mass Spectrom. 1990, 19, 475.
    • (1990) Biomed. Environ. Mass Spectrom. , vol.19 , pp. 475
    • Von, S.D.1    Kulik, W.2    Heerma, W.3
  • 31
    • 84989031229 scopus 로고
    • New rules concerning the formation of protonated amino acids from protonated dipeptides using the proton affinity order determined from collisionally activated decomposition spectra
    • K. Isa, T. Omote, M. Ayama,. New rules concerning the formation of protonated amino acids from protonated dipeptides using the proton affinity order determined from collisionally activated decomposition spectra. Org. Mass Spectrom. 1990, 25, 620.
    • (1990) Org. Mass Spectrom. , vol.25 , pp. 620
    • Isa, K.1    Omote, T.2    Ayama, M.3
  • 32
    • 78650713951 scopus 로고    scopus 로고
    • α-Fmoc-protected ureidopeptides by electrospray ionization tandem mass spectrometry (ESI-MS/MS): Differentiation of positional isomers
    • α-Fmoc-protected ureidopeptides by electrospray ionization tandem mass spectrometry (ESI-MS/MS): differentiation of positional isomers. J. Mass Spectrom. 2010, 45, 1461.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 1461
    • Ramesh, M.1    Raju, B.2    Srinivas, R.3    Sureshbabu, V.V.4    Narendra, N.5    Vasantha, B.6
  • 33
    • 33749849935 scopus 로고    scopus 로고
    • Rearrangement mechanism of the sodium adducts of Fmoc protected amino acids
    • D. Jintang, L. Yanmei, Z. Zhentai, C. Yi, Z. Yufen,. Rearrangement mechanism of the sodium adducts of Fmoc protected amino acids. Chin. Sci. Bull. 2003, 48, 2317.
    • (2003) Chin. Sci. Bull. , vol.48 , pp. 2317
    • Jintang, D.1    Yanmei, L.2    Zhentai, Z.3    Yi, C.4    Yufen, Z.5
  • 34
    • 34247539933 scopus 로고    scopus 로고
    • Anew fragmentation rearrangement of the N-terminal protected amino acids using ESI-MS/MS
    • Z. T. Zhu, Y. M. Li, Y. T. Guo, M. Sun, Y. F. Zhao,. Anew fragmentation rearrangement of the N-terminal protected amino acids using ESI-MS/MS. Indian J. Biochem. Biophys. 2006, 43, 372.
    • (2006) Indian J. Biochem. Biophys. , vol.43 , pp. 372
    • Zhu, Z.T.1    Li, Y.M.2    Guo, Y.T.3    Sun, M.4    Zhao, Y.F.5
  • 35
    • 0031721179 scopus 로고    scopus 로고
    • Time-of-flight secondary ion mass spectrometry of Fmoc-amino acids linked to solid supports through ionic interactions
    • C. Enjalbal, J. Martinez, G. Subra, R. Combarieu, J. L. Aubagnac,. Time-of-flight secondary ion mass spectrometry of Fmoc-amino acids linked to solid supports through ionic interactions. Rapid Commun. Mass Spectrom. 1998, 12, 1715.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 1715
    • Enjalbal, C.1    Martinez, J.2    Subra, G.3    Combarieu, R.4    Aubagnac, J.L.5
  • 37
    • 0042198946 scopus 로고    scopus 로고
    • Energetics of an intracluster β-elimination process driven by acetate anions. The case of a Fmoc-protected peptide investigated by high-resolution electrospray ionization tandem mass spectrometry
    • L. Di Donna, A. Liguori, A. Napoli, G. Sindona,. Energetics of an intracluster β-elimination process driven by acetate anions. The case of a Fmoc-protected peptide investigated by high-resolution electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 2003, 38, 778.
    • (2003) J. Mass Spectrom. , vol.38 , pp. 778
    • Di Donna, L.1    Liguori, A.2    Napoli, A.3    Sindona, G.4
  • 38
    • 0031743498 scopus 로고    scopus 로고
    • Application of time-of-flight secondary ion mass spectrometry to in situ monitoring of solid-phase peptide synthesis on the multipin™ system
    • J. L. Aubagnac, C. Enjalbal, G. Subra, A. M. Bray, R. Combarieu, J. Martinez,. Application of time-of-flight secondary ion mass spectrometry to in situ monitoring of solid-phase peptide synthesis on the multipin™ system. J. Mass Spectrom. 1998, 33, 1094.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 1094
    • Aubagnac, J.L.1    Enjalbal, C.2    Subra, G.3    Bray, A.M.4    Combarieu, R.5    Martinez, J.6
  • 39
    • 0032783369 scopus 로고    scopus 로고
    • Imaging time-of-flight secondary ion mass spectrometry of solid-phase peptide syntheses
    • J. L. Aubagnac, C. Enjalbal, C. Drouot, R. Combarieu, J. Martinez,. Imaging time-of-flight secondary ion mass spectrometry of solid-phase peptide syntheses. J. Mass Spectrom. 1999, 34, 749.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 749
    • Aubagnac, J.L.1    Enjalbal, C.2    Drouot, C.3    Combarieu, R.4    Martinez, J.5
  • 40
    • 42249099173 scopus 로고    scopus 로고
    • α-Fmoc protected amino/peptidyl weinreb amides employing acid chlorides as key intermediates
    • α-Fmoc protected amino/peptidyl weinreb amides employing acid chlorides as key intermediates. ARKIVOC 2008 (ii) 243.
    • (2008) ARKIVOC , vol.2 , pp. 243
    • Sureshbabu, V.V.1    Hemantha, H.P.2
  • 41
    • 0032564614 scopus 로고    scopus 로고
    • Synthesis of peptides employing Fmoc-amino acid chlorides and commercial zinc dust
    • (a),.
    • (a), H. N. Gopi, V. V. Sureshbabu,. Synthesis of peptides employing Fmoc-amino acid chlorides and commercial zinc dust. Tetrahedron Lett. 1998, 39, 9769
    • (1998) Tetrahedron Lett. , vol.39 , pp. 9769
    • Gopi, H.N.1    Sureshbabu, V.V.2
  • 42
    • 0035083123 scopus 로고    scopus 로고
    • Deprotonation of hydrochloride salts of amino acid esters and peptide esters using commercial zinc dust
    • (b),.
    • (b), K. Ananda, V. V. Sureshbau,. Deprotonation of hydrochloride salts of amino acid esters and peptide esters using commercial zinc dust. J. Pept. Res. 2001, 57, 223.
    • (2001) J. Pept. Res. , vol.57 , pp. 223
    • Ananda, K.1    Sureshbau, V.V.2
  • 43
    • 33845375891 scopus 로고
    • (Fluoren-9-ylmethoxy)carbonyl (Fmoc) amino acid chlorides. Synthesis, characterization, and application to the rapid synthesis of short peptide segments
    • (a),.
    • (a), L. A. Carpino, B. J. Cohen, K. E. Stephens Jr, S. Y. Sadat-Aalaee, J. H. Tien, D. C. Langridge,. (Fluoren-9-ylmethoxy)carbonyl (Fmoc) amino acid chlorides. Synthesis, characterization, and application to the rapid synthesis of short peptide segments. J. Org. Chem. 1986, 51, 3732
    • (1986) J. Org. Chem. , vol.51 , pp. 3732
    • Carpino, L.A.1    Cohen, B.J.2    Stephens Jr., K.E.3    Sadat-Aalaee, S.Y.4    Tien, J.H.5    Langridge, D.C.6
  • 44
    • 0242500436 scopus 로고    scopus 로고
    • Synthesis of Fmoc-amino acid chlorides assisted by ultrasonication, a rapid approach
    • (b),.
    • (b), Kantharaju, B. S. Patil, V. V. Sureshbau,. Synthesis of Fmoc-amino acid chlorides assisted by ultrasonication, a rapid approach. Lett. Pept. Sci. 2002, 9, 227.
    • (2002) Lett. Pept. Sci. , vol.9 , pp. 227
    • Kantharaju1    Patil, B.S.2    Sureshbau, V.V.3
  • 45
    • 0032500102 scopus 로고    scopus 로고
    • 2. Applications in peptide synthesis
    • 2. Applications in peptide synthesis. Tetrahedron Lett. 1998, 39, 5031.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 5031
    • Pascal, R.1    Sola, R.2
  • 46
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • P. Roepstorff, J. Fohlman,. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed. Mass Spectrom. 1984, 11, 601.
    • (1984) Biomed. Mass Spectrom. , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 47
    • 0023804303 scopus 로고
    • Contribution of mass spectrometry to peptide and protein structure
    • K. Biemann,. Contribution of mass spectrometry to peptide and protein structure. Biomed. Environ. Mass Spectrom. 1988, 16, 99.
    • (1988) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 99
    • Biemann, K.1
  • 48
    • 84994921866 scopus 로고
    • Mass spectrometric determination of the amino acid sequence of peptides and proteins
    • K. Biemann, S. A. Martin,. Mass spectrometric determination of the amino acid sequence of peptides and proteins. Mass Spectrom. Rev. 1987, 6, 1.
    • (1987) Mass Spectrom. Rev. , vol.6 , pp. 1
    • Biemann, K.1    Martin, S.A.2
  • 50
    • 0002298708 scopus 로고
    • Aziridinone and 2-azetidinone and their protonated structures. An ab intio molecular orbital study making comparisons with bridgehead bicyclic lactams and acetamide
    • A. Greenberg, H. J. Hsing, J. L. Liebman,. Aziridinone and 2-azetidinone and their protonated structures. An ab intio molecular orbital study making comparisons with bridgehead bicyclic lactams and acetamide. J. Mol. Struct. Theochem 1995, 338, 83.
    • (1995) J. Mol. Struct. Theochem , vol.338 , pp. 83
    • Greenberg, A.1    Hsing, H.J.2    Liebman, J.L.3
  • 52
    • 33747143360 scopus 로고    scopus 로고
    • Fragmentation reactions of deprotonated peptides containing aspartic acid
    • A. G. Harrision, A. B. Young,. Fragmentation reactions of deprotonated peptides containing aspartic acid. Int. J. Mass Spectrom. 2006, 255, 111.
    • (2006) Int. J. Mass Spectrom. , vol.255 , pp. 111
    • Harrision, A.G.1    Young, A.B.2
  • 53
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • R. A. Zubarev, N. L. Kelleher, F. W. McLafferty,. Electron capture dissociation of multiply charged protein cations. A nonergodic process. J. Am. Chem. Soc. 1998, 120, 3265.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3265
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.