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Volumn 1, Issue 2, 1996, Pages 157-165

Solution conformation of an immunogenic peptide derived from the principal neutralizing determinant of the HIV-2 envelope glycoprotein gp125

Author keywords

HIV 2; Peplide vaccine; Peptide conformation

Indexed keywords

DISULFIDE; HIV 2 ENVELOPE PROTEIN GP125; HIV-2 ENVELOPE PROTEIN GP125; HUMAN IMMUNODEFICIENCY VIRUS ANTIGEN; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; PEPTIDE; PROTEIN PRECURSOR; RECOMBINANT VACCINE; VIRUS ENVELOPE PROTEIN;

EID: 0030334731     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00024-7     Document Type: Article
Times cited : (12)

References (53)
  • 1
    • 0041914944 scopus 로고
    • Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope gp120
    • Rusche, J.R., et al., & Matthews, T.J. (1988). Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope gp120. Proc. Natl. Acad. Sci. USA 85, 3198-3202.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3198-3202
    • Rusche, J.R.1    Matthews, T.J.2
  • 2
    • 0043080631 scopus 로고
    • Human immunodeficiency virus type 1 neutralization epitope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees
    • Goudsmit, J., et al., & Gajdusek, D.C. (1988). Human immunodeficiency virus type 1 neutralization epitope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees. Proc. Natl. Acad. Sci. USA 85, 4478-4482.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4478-4482
    • Goudsmit, J.1    Gajdusek, D.C.2
  • 3
    • 0024121522 scopus 로고
    • Type-specific neutralization of the human immunodeficiency virus with antibodies to env-encoded synthetic peptides
    • Palker, T.J., et al., & Haynes, B.F. (1988). Type-specific neutralization of the human immunodeficiency virus with antibodies to env-encoded synthetic peptides. Proc. Natl. Acad. Sci. USA 85, 1932-1936.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1932-1936
    • Palker, T.J.1    Haynes, B.F.2
  • 4
    • 0005848581 scopus 로고
    • Principal neutralizing domain of the human immunodeficiency virus type 1 envelope protein
    • Javaherian, K., et al., & Matthews, T.J. (1989). Principal neutralizing domain of the human immunodeficiency virus type 1 envelope protein. Proc. Natl. Acad. Sci. USA 86, 6768-6772.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6768-6772
    • Javaherian, K.1    Matthews, T.J.2
  • 5
    • 0025745088 scopus 로고
    • Hyperimmune antisera against synthetic peptides representing the glycoprotein of human immunodeficiency virus type 2 can mediate neutralization and antibody-dependent cytotoxic activity
    • Björling, E., et al., & Norrby, E. (1991). Hyperimmune antisera against synthetic peptides representing the glycoprotein of human immunodeficiency virus type 2 can mediate neutralization and antibody-dependent cytotoxic activity. Proc. Natl. Acad. Sci. USA 88, 6082-6086.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6082-6086
    • Björling, E.1    Norrby, E.2
  • 6
    • 0028328770 scopus 로고
    • Two neutralizing domains in the V3 region in the envelope glycoprotein gp125 of human immunodeficiency virus type 2.7
    • Björling, E., Chiodi, F., Utter, G. & Norrby, E. (1994). Two neutralizing domains in the V3 region in the envelope glycoprotein gp125 of human immunodeficiency virus type 2.7. Immunol. 152, 1952-1959.
    • (1994) Immunol. , vol.152 , pp. 1952-1959
    • Björling, E.1    Chiodi, F.2    Utter, G.3    Norrby, E.4
  • 7
    • 33645858485 scopus 로고
    • Conserved sequence and structural elements in the HIV-1 principal neutralizing domain
    • LaRosa, G.J., et al., & Putney, S.D. (1990). Conserved sequence and structural elements in the HIV-1 principal neutralizing domain. Science 24, 9932-9935.
    • (1990) Science , vol.24 , pp. 9932-9935
    • LaRosa, G.J.1    Putney, S.D.2
  • 8
    • 0022878540 scopus 로고
    • Restricted neutralization of divergent human T-lymphotropic virus type III isolates by antibodies to the major envelope glycoprotein
    • Matthews, T.J., et al., & Bolognesi, D.P. (1986). Restricted neutralization of divergent human T-lymphotropic virus type III isolates by antibodies to the major envelope glycoprotein. Proc. Natl. Acad. Sci. USA 83, 9709-9713.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9709-9713
    • Matthews, T.J.1    Bolognesi, D.P.2
  • 9
    • 0022995585 scopus 로고
    • HTLV-III/LAV-neutralizing antibodies to an E. coli-produced fragment of the virus envelope
    • Putney, S.D., et al., & Bolognesi, D.P. (1986). HTLV-III/LAV-neutralizing antibodies to an E. coli-produced fragment of the virus envelope. Science 234, 1392-1395.
    • (1986) Science , vol.234 , pp. 1392-1395
    • Putney, S.D.1    Bolognesi, D.P.2
  • 10
    • 33645867921 scopus 로고
    • Biological phenotype of HIV-2 isolates correlates with V3 genotype
    • in press
    • Albert, J., et al., & Chiodi, F. (1995). Biological phenotype of HIV-2 isolates correlates with V3 genotype. AIDS Res. Hum. Retrovir. in press.
    • (1995) AIDS Res. Hum. Retrovir.
    • Albert, J.1    Chiodi, F.2
  • 11
    • 0028998243 scopus 로고
    • Neutralizing monoclonal antibodies against human immunodeficiency virus type 2 gp120
    • Matsushita, S., Matsumi, S., Yoshimura, K., Morikita, T., Murakami, T. & Takatsuki, K. (1995). Neutralizing monoclonal antibodies against human immunodeficiency virus type 2 gp120. J. Virol. 69, 3333-3340.
    • (1995) J. Virol. , vol.69 , pp. 3333-3340
    • Matsushita, S.1    Matsumi, S.2    Yoshimura, K.3    Morikita, T.4    Murakami, T.5    Takatsuki, K.6
  • 12
    • 0026002948 scopus 로고
    • Solution conformational preferences of immunogenic peptides derived from the principal neutralizing determinant of the HIV-1 envelope glycoprotein gp120
    • Chandrasekhar, K., Profy, A.T. & Dyson, H.J. (1991). Solution conformational preferences of immunogenic peptides derived from the principal neutralizing determinant of the HIV-1 envelope glycoprotein gp120. Biochemistry 30, 9187-9194.
    • (1991) Biochemistry , vol.30 , pp. 9187-9194
    • Chandrasekhar, K.1    Profy, A.T.2    Dyson, H.J.3
  • 13
    • 0026753361 scopus 로고
    • Solution conformation of a peptide corresponding to the principal neutralizing determinant of HIV-1IIIB: A two-dimensional NMR study
    • Zvi, A., Hiller, R. & Anglister, J. (1992). Solution conformation of a peptide corresponding to the principal neutralizing determinant of HIV-1IIIB: a two-dimensional NMR study. Biochemistry 31, 6972-6979.
    • (1992) Biochemistry , vol.31 , pp. 6972-6979
    • Zvi, A.1    Hiller, R.2    Anglister, J.3
  • 14
    • 0026642502 scopus 로고
    • Synthesis and conformational studies of N-glycosylated analogues of the HIV-1 principal neutralizing determinant
    • Laczko, I., et al., & Ötvös, L.J. (1992). Synthesis and conformational studies of N-glycosylated analogues of the HIV-1 principal neutralizing determinant. Biochemistry 31, 4282-4288.
    • (1992) Biochemistry , vol.31 , pp. 4282-4288
    • Laczko, I.1    Ötvös, L.J.2
  • 16
    • 0028355519 scopus 로고
    • NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus
    • De Lorimier, R., Moody, M.A., Haynes, B.F. & Spicer, L.D. (1994). NMR-derived solution conformations of a hybrid synthetic peptide containing multiple epitopes of envelope protein gp120 from the RF strain of human immunodeficiency virus. Biochemistry 33, 2055-2062.
    • (1994) Biochemistry , vol.33 , pp. 2055-2062
    • De Lorimier, R.1    Moody, M.A.2    Haynes, B.F.3    Spicer, L.D.4
  • 17
    • 0027325038 scopus 로고
    • Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen
    • Rini, J.M., Stanfield, R.L, Stura, E.A., Salinas, P.A., Profy, A.T. & Wilson, I.A. (1993). Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen. Proc. Natl. Acad. Sci. USA 90, 6325-6329.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6325-6329
    • Rini, J.M.1    Stanfield, R.L.2    Stura, E.A.3    Salinas, P.A.4    Profy, A.T.5    Wilson, I.A.6
  • 18
  • 19
    • 0024316091 scopus 로고
    • Conformation of a T cell stimulating peptide in aqueous solution
    • Waltho, J.P., Feher, V.A., Lerner, R.A. & Wright, P.E. (1989). Conformation of a T cell stimulating peptide in aqueous solution. FEBS Lett. 250, 400-404.
    • (1989) FEBS Lett. , vol.250 , pp. 400-404
    • Waltho, J.P.1    Feher, V.A.2    Lerner, R.A.3    Wright, P.E.4
  • 20
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- And H-helices of myoglobin
    • Waltho, J.P., Feher, V.A., Merutka, G., Dyson, H.J. & Wright, P.E. (1993). Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry 32, 6337-6347.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Merutka, G.3    Dyson, H.J.4    Wright, P.E.5
  • 21
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. 1. Sequence requirements for the formation of a reverse turn
    • Dyson, H.J., Rance, M., Houghten, R.A., Lerner, R.A. & Wright, P.E. (1988). Folding of immunogenic peptide fragments of proteins in water solution. 1. Sequence requirements for the formation of a reverse turn. J. Mol. Biol. 201, 161-200.
    • (1988) J. Mol. Biol. , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Lerner, R.A.4    Wright, P.E.5
  • 23
    • 0025904730 scopus 로고
    • Defining solution conformations of small linear peptides
    • Dyson, H.J. & Wright, P.E. (1991). Defining solution conformations of small linear peptides. Annu. Rev. Biophys. Biophys. Chem. 20, 519-538.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 519-538
    • Dyson, H.J.1    Wright, P.E.2
  • 24
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D.S., Sykes, B.D. & Richards, P.M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, P.M.3
  • 25
    • 0029207339 scopus 로고
    • Peptide proton random coil chemical shifts obtained as a function of temperature and trifluoroethanol concentration
    • Merutka, G., Dyson, H.J. & Wright, P.E. (1995). Peptide proton random coil chemical shifts obtained as a function of temperature and trifluoroethanol concentration. J. Biomol. NMR 5, 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 26
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C
    • Gagné, S.M., Tsuda, S., Li, M.X., Chandra, M., Smillie, L.B. & Sykes, B.D. (1994). Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 3, 1961-1974.
    • (1994) Protein Sci. , vol.3 , pp. 1961-1974
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Chandra, M.4    Smillie, L.B.5    Sykes, B.D.6
  • 27
    • 0017189603 scopus 로고
    • The X-Pro peptide bond as an NMR probe for conformational studies of flexible linear peptides
    • Grathwohl, C. & Wüthrich, K. (1976). The X-Pro peptide bond as an NMR probe for conformational studies of flexible linear peptides. Biopolymers 15, 2025-2041.
    • (1976) Biopolymers , vol.15 , pp. 2025-2041
    • Grathwohl, C.1    Wüthrich, K.2
  • 28
    • 0028068045 scopus 로고
    • Stabilization of a type VI turn in a family of linear peptides in water solution
    • Yao, J., Feher, V.A., Espejo, B.F., Reymond, M.T., Wright, P.E. & Dyson, H.J. (1994). Stabilization of a type VI turn in a family of linear peptides in water solution. J. Mol. Biol. 243, 736-753.
    • (1994) J. Mol. Biol. , vol.243 , pp. 736-753
    • Yao, J.1    Feher, V.A.2    Espejo, B.F.3    Reymond, M.T.4    Wright, P.E.5    Dyson, H.J.6
  • 30
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. (1981). The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 32
    • 0025321903 scopus 로고
    • Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å
    • Stanfield, R.L., Fieser, T.M., Lerner, R.A. & Wilson, I.A. (1990). Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å. Science 248, 712-719.
    • (1990) Science , vol.248 , pp. 712-719
    • Stanfield, R.L.1    Fieser, T.M.2    Lerner, R.A.3    Wilson, I.A.4
  • 33
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini, J.M., Schulze-Gahmen, U. & Wilson, I.A. (1992). Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science 255, 959-965.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 34
    • 0026757989 scopus 로고
    • Three-dimensional structure of an angiotensin II-Fab complex at 3 A: Hormone recognition by an anti-idiotypic antibody
    • Garcia, K.C., Ronco, P.M., Verroust, P.J., Brünger, A.T. & Amzel, L.M. (1992). Three-dimensional structure of an angiotensin II-Fab complex at 3 A: hormone recognition by an anti-idiotypic antibody. Science 257, 502-507.
    • (1992) Science , vol.257 , pp. 502-507
    • Garcia, K.C.1    Ronco, P.M.2    Verroust, P.J.3    Brünger, A.T.4    Amzel, L.M.5
  • 35
    • 0027301875 scopus 로고
    • Crystal structure of an anticholera toxin peptide complex at 2.3 Å
    • Shoham, M. (1993). Crystal structure of an anticholera toxin peptide complex at 2.3 Å. J. Mol. Biol. 232, 1169-1175.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1169-1175
    • Shoham, M.1
  • 36
    • 0028304866 scopus 로고
    • Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2
    • Tormo, J., Blass, D., Parry, N.R., Rowlands, D., Stuart, D. & Fita, I. (1994). Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2. EMBOJ. 13, 2247-2256.
    • (1994) EMBOJ. , vol.13 , pp. 2247-2256
    • Tormo, J.1    Blass, D.2    Parry, N.R.3    Rowlands, D.4    Stuart, D.5    Fita, I.6
  • 37
    • 0022394507 scopus 로고
    • The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn
    • Dyson, H.J., Cross, K.J., Houghten, R.A., Wilson, I.A., Wright, P.E. & Lerner, R.A. (1985). The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn. Nature 318, 480-483.
    • (1985) Nature , vol.318 , pp. 480-483
    • Dyson, H.J.1    Cross, K.J.2    Houghten, R.A.3    Wilson, I.A.4    Wright, P.E.5    Lerner, R.A.6
  • 38
    • 0024278572 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix
    • Dyson, H.J., Rance, M., Houghten, R.A., Wright, P.E. & Lerner, R.A. (1988). Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J. Mol. Biol. 201, 201-217.
    • (1988) J. Mol. Biol. , vol.201 , pp. 201-217
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Wright, P.E.4    Lerner, R.A.5
  • 39
    • 0026483948 scopus 로고
    • A β-turn is present in the 392-411 segment of the human fibrinogen γ-chain. Effects of structural changes in this segment on affinity to antibody 4A5
    • Blumenstein, M., Matsueda, G.R., Timmons, S. & Hawiger, J. (1992). A β-turn is present in the 392-411 segment of the human fibrinogen γ-chain. Effects of structural changes in this segment on affinity to antibody 4A5. Biochemistry 31, 10692-10698.
    • (1992) Biochemistry , vol.31 , pp. 10692-10698
    • Blumenstein, M.1    Matsueda, G.R.2    Timmons, S.3    Hawiger, J.4
  • 40
    • 0026770069 scopus 로고
    • Induced peptide conformations in different antibody complexes: Molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints
    • Scherf, T., Hiller, R., Naider, F., Levitt, M. & Anglister, J. (1992). Induced peptide conformations in different antibody complexes: molecular modeling of the three-dimensional structure of peptide-antibody complexes using NMR-derived distance restraints. Biochemistry 31, 6884-6897.
    • (1992) Biochemistry , vol.31 , pp. 6884-6897
    • Scherf, T.1    Hiller, R.2    Naider, F.3    Levitt, M.4    Anglister, J.5
  • 41
    • 0027743316 scopus 로고
    • NMR solution structure and flexibility of a peptide antigen representing the receptor binding domain of Pseudomonas aeruginosa
    • McInnes, C., Sönnichsen, F.D., Kay, C.M., Hodges, R.S. & Sykes, B.D. (1993). NMR solution structure and flexibility of a peptide antigen representing the receptor binding domain of Pseudomonas aeruginosa. Biochemistry 32, 13432-13440.
    • (1993) Biochemistry , vol.32 , pp. 13432-13440
    • McInnes, C.1    Sönnichsen, F.D.2    Kay, C.M.3    Hodges, R.S.4    Sykes, B.D.5
  • 42
    • 0029588199 scopus 로고
    • Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7 and PAK: Implications for receptor binding and synthetic vaccine design
    • Campbell, A.P., McInnes, C., Hodges, R.S. & Sykes, B.D. (1995). Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7 and PAK: implications for receptor binding and synthetic vaccine design, Biochemistry 34, 16255-16268.
    • (1995) Biochemistry , vol.34 , pp. 16255-16268
    • Campbell, A.P.1    McInnes, C.2    Hodges, R.S.3    Sykes, B.D.4
  • 43
    • 0025848453 scopus 로고
    • Synthesis, conformational properties and antibody recognition of peptides containing β-turn mimetics based on α-alkylproline
    • Hinds, H.G., et al., & Robinson, J.A. (1991). Synthesis, conformational properties and antibody recognition of peptides containing β-turn mimetics based on α-alkylproline. J. Med. Chem. 34, 1777-1789.
    • (1991) J. Med. Chem. , vol.34 , pp. 1777-1789
    • Hinds, H.G.1    Robinson, J.A.2
  • 44
    • 0025292473 scopus 로고
    • Epitopes recognized by the neutralizing antibodies of an HIV-1 infected individual
    • Profy, A.T., Saunas, P.A., Eckler, L.I., Dunlop, N.M., Nara, P.L. & Putney, S.D. (1990). Epitopes recognized by the neutralizing antibodies of an HIV-1 infected individual. J. Immunol. 144, 4641-4647.
    • (1990) J. Immunol. , vol.144 , pp. 4641-4647
    • Profy, A.T.1    Saunas, P.A.2    Eckler, L.I.3    Dunlop, N.M.4    Nara, P.L.5    Putney, S.D.6
  • 45
    • 0027103030 scopus 로고
    • Antigen-antibody interactions: Elucidation of the epitope and strain-specificity of a monoclonal antibody directed against the pilin protein adherence binding domain of Pseudomonas aeruginosa strain K
    • Wong, W.Y., Irwin, R.T., Paranchych, W. & Hodges, R.S. (1992). Antigen-antibody interactions: elucidation of the epitope and strain-specificity of a monoclonal antibody directed against the pilin protein adherence binding domain of Pseudomonas aeruginosa strain K. Protein Sci. 1, 1308-1318.
    • (1992) Protein Sci. , vol.1 , pp. 1308-1318
    • Wong, W.Y.1    Irwin, R.T.2    Paranchych, W.3    Hodges, R.S.4
  • 46
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Serensen, O.W. & Ernst, R.R. (1982). Multiple quantum filters for elucidating NMR coupling networks. J. Am. Chem. Soc. 104, 6800-6801.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Serensen, O.W.2    Ernst, R.R.3
  • 48
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D.G. (1985). MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 49
    • 45949117739 scopus 로고
    • Improved techniques for homonuclear rotating-frame and isotropic mixing experiments
    • Rance, M. (1987). Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J. Magn. Reson. 74, 557-564.
    • (1987) J. Magn. Reson. , vol.74 , pp. 557-564
    • Rance, M.1
  • 50
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P. & Ernst, R.R. (1979). Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 51
    • 84915716471 scopus 로고
    • Elucidation of cross-relaxation in liquids by two-dimensional N.M.R. spectroscopy
    • Macura, S. & Ernst, R.R. (1980). Elucidation of cross-relaxation in liquids by two-dimensional N.M.R. spectroscopy. Mol. Phys. 41, 95-117.
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 52
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D.J., Haberkorn, R.A. & Ruben, D.J. (1982). A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48, 286-292.
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3


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