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Volumn 33, Issue SUPPL. 2, 1998, Pages 28-37

Application of electrospray ionization mass spectrometry for studying human immunodeficiency virus protein complexes

Author keywords

Electrospray ionization mass spectrometry; Integrase; Noncovalent complexes; Nucleocapsid protein; Protease

Indexed keywords

CAPSID PROTEIN; INTEGRASE; PROTEINASE; RNA; VIRUS PROTEIN; ZINC FINGER PROTEIN; GAG PROTEIN; NCP7 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; PEPSTATIN; PROTEINASE INHIBITOR; STREPTOMYCES PEPSIN INHIBITOR; ZINC;

EID: 0032246514     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(1998)33:2+<28::AID-PROT5>3.0.CO;2-Y     Document Type: Article
Times cited : (29)

References (51)
  • 1
    • 0001401150 scopus 로고
    • Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry
    • Katta, V., Chait, B.T. Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry. J. Am. Chem. Soc. 113:8534-8535, 1991.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 8534-8535
    • Katta, V.1    Chait, B.T.2
  • 2
    • 0001413545 scopus 로고
    • Detection of noncovalent receptor-ligand complexes by mass spectrometry
    • Ganem, B., Li, Y.-T., Henion, J.D. Detection of noncovalent receptor-ligand complexes by mass spectrometry. J. Am. Chem. Soc. 113:6294-6296, 1991.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6294-6296
    • Ganem, B.1    Li, Y.-T.2    Henion, J.D.3
  • 3
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J.A. 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.A.1
  • 4
    • 3542997762 scopus 로고    scopus 로고
    • Optimized procedures for purification and solubilization of basic fibroblast growth factor inclusion bodies
    • Estape, D., Rinas, U. Optimized procedures for purification and solubilization of basic fibroblast growth factor inclusion bodies. Biotechnol. Tech. 10:481-484, 1996.
    • (1996) Biotechnol. Tech. , vol.10 , pp. 481-484
    • Estape, D.1    Rinas, U.2
  • 6
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C., Von Hippel, P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326, 1989.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 8
    • 0002012936 scopus 로고
    • A strategy for characterizing new viral proteases: Applied to HIV PR and HAV 3C PR
    • Schneider, C.H., Eberle, A.N., (eds.). Leiden, The Netherlands: ESCOM
    • Pennington, M.W., Zaydenberg, I., Byrnes, M.E., et al. A strategy for characterizing new viral proteases: Applied to HIV PR and HAV 3C PR. In: "Peptides 1992, Proceedings of the 22nd European Peptide Symposium." Schneider, C.H., Eberle, A.N., (eds.). Leiden, The Netherlands: ESCOM, 1993:936-937.
    • (1993) Peptides 1992, Proceedings of the 22nd European Peptide Symposium , pp. 936-937
    • Pennington, M.W.1    Zaydenberg, I.2    Byrnes, M.E.3
  • 9
    • 0030019808 scopus 로고    scopus 로고
    • The in vitro ejection of zinc from human immunodeficiency virus (HIV) type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity
    • Tummino, P.J., Scholten, J.D., Harvey, P.J., et al. The in vitro ejection of zinc from human immunodeficiency virus (HIV) type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity. Proc. Natl. Acad. Sci. USA 93:969-973, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 969-973
    • Tummino, P.J.1    Scholten, J.D.2    Harvey, P.J.3
  • 10
    • 0001962888 scopus 로고
    • Molecular mass measurement of intact ribonucleic acids via electrospray ionization quadrupole mass spectrometry
    • Limbach, P.A., Crain, P.F., McCloskey, J.A. Molecular mass measurement of intact ribonucleic acids via electrospray ionization quadrupole mass spectrometry. J. Am. Soc. Mass Spectrom. 6:27-39, 1995.
    • (1995) J. Am. Soc. Mass Spectrom. , vol.6 , pp. 27-39
    • Limbach, P.A.1    Crain, P.F.2    McCloskey, J.A.3
  • 11
    • 0031573676 scopus 로고    scopus 로고
    • HIV-1 tat peptide binding to TAR RNA by electrospray ionization mass spectrometry
    • Sannes-Lowery, K.A., Hu, P., Mack, D.P., Mei, H.-Y., Loo, J.A. HIV-1 tat peptide binding to TAR RNA by electrospray ionization mass spectrometry. Anal. Chem. 69:5130-5135, 1997.
    • (1997) Anal. Chem. , vol.69 , pp. 5130-5135
    • Sannes-Lowery, K.A.1    Hu, P.2    Mack, D.P.3    Mei, H.-Y.4    Loo, J.A.5
  • 12
    • 84989056711 scopus 로고
    • Primary to quaternary protein structure determination with electrospray ionization and magnetic sector mass spectrometry
    • Loo, J.A., Ogorzalek Loo, R.R., Andrews, P.C. Primary to quaternary protein structure determination with electrospray ionization and magnetic sector mass spectrometry. Org. Mass Spectrom. 28:1640-1649, 1993.
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1640-1649
    • Loo, J.A.1    Ogorzalek Loo, R.R.2    Andrews, P.C.3
  • 13
    • 0028149331 scopus 로고
    • Sensitive and selective determination of proteins with electrospray ionization magnetic sector mass spectrometry and array detection
    • Loo, J.A., Pesch, R. Sensitive and selective determination of proteins with electrospray ionization magnetic sector mass spectrometry and array detection. Anal. Chem. 66: 3659-3663, 1994.
    • (1994) Anal. Chem. , vol.66 , pp. 3659-3663
    • Loo, J.A.1    Pesch, R.2
  • 14
    • 0013410944 scopus 로고
    • Applying charge discrimination with electrospray ionization-mass spectrometry to protein analysis
    • Loo, J.A., Ogorzalek Loo, R.R. Applying charge discrimination with electrospray ionization-mass spectrometry to protein analysis. J. Am. Soc. Mass Spectrom. 6:1098-1104, 1995.
    • (1995) J. Am. Soc. Mass Spectrom. , vol.6 , pp. 1098-1104
    • Loo, J.A.1    Ogorzalek Loo, R.R.2
  • 15
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J.B., Mann, M., Meng, C.K., Wong, S.F., Whitehouse, C.M. Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71, 1989.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 17
    • 0030902816 scopus 로고    scopus 로고
    • HIV integrase: A target for AIDS therapeutics
    • Thomas, M., Brady, L. HIV integrase: a target for AIDS therapeutics. Trends Biotechnol. 15:167-172, 1997.
    • (1997) Trends Biotechnol. , vol.15 , pp. 167-172
    • Thomas, M.1    Brady, L.2
  • 18
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, F., Hickman, A.B., Jenkins, T.M., Engelman, A., Craigie, R., Davies, D.R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266:1981-1986, 1994.
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 19
    • 0027973067 scopus 로고
    • Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase
    • Hickman, A.B., Palmer, I., Engelman, A., Craigie, R., Wingfield, P. Biophysical and enzymatic properties of the catalytic domain of HIV-1 integrase. J. Biol. Chem. 269: 29279-29287, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29279-29287
    • Hickman, A.B.1    Palmer, I.2    Engelman, A.3    Craigie, R.4    Wingfield, P.5
  • 20
    • 0029980485 scopus 로고    scopus 로고
    • A soluble active mutant of HIV-1 integrase. Involvement of both the core and carboxyl-terminal domains in multimerization
    • Jenkins, T.M., Engelman, A., Ghirlando, R., Craigie, R. A soluble active mutant of HIV-1 integrase. Involvement of both the core and carboxyl-terminal domains in multimerization. J. Biol. Chem. 271:7712-7718, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 21
    • 0028447420 scopus 로고
    • Observation of the noncovalent quaternary associations of proteins by electrospray ionization mass spectrometry
    • Light-Wahl, K.J., Schwartz, B.L., Smith, R.D. Observation of the noncovalent quaternary associations of proteins by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 116:5271-5278, 1994.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5271-5278
    • Light-Wahl, K.J.1    Schwartz, B.L.2    Smith, R.D.3
  • 22
    • 0027461675 scopus 로고
    • Tandem mass spectrometry of very large molecules. 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization
    • Loo, J.A., Edmonds, C.G., Smith, R.D. Tandem mass spectrometry of very large molecules. 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization. Anal. Chem. 65:425-438, 1993.
    • (1993) Anal. Chem. , vol.65 , pp. 425-438
    • Loo, J.A.1    Edmonds, C.G.2    Smith, R.D.3
  • 23
    • 0024412506 scopus 로고
    • Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease
    • Wlodawer, A., Miller, M., Jaskolski, M., et al. Conserved folding in retroviral proteases: Crystal structure of a synthetic HIV-1 protease. Science 245:616-621, 1989.
    • (1989) Science , vol.245 , pp. 616-621
    • Wlodawer, A.1    Miller, M.2    Jaskolski, M.3
  • 24
    • 0029859529 scopus 로고    scopus 로고
    • Ionization states of the catalytic residues in HIV-1 protease
    • Smith, R., Brereton, I.M., Chai, R.Y., Kent, S.B.H. Ionization states of the catalytic residues in HIV-1 protease. Nat. Struct. Biol. 3:946-950., 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 946-950
    • Smith, R.1    Brereton, I.M.2    Chai, R.Y.3    Kent, S.B.H.4
  • 25
    • 0027957967 scopus 로고
    • Dissociation and association of the HIV-1 protease dimer subunits: Equilibrium and rates
    • Darke, P.L., Jordan, S.P., Hall, D.L., Zugay, J.A., Shafer, J.A., Kuo, L.C. Dissociation and association of the HIV-1 protease dimer subunits: equilibrium and rates. Biochemistry 33:98-105, 1994.
    • (1994) Biochemistry , vol.33 , pp. 98-105
    • Darke, P.L.1    Jordan, S.P.2    Hall, D.L.3    Zugay, J.A.4    Shafer, J.A.5    Kuo, L.C.6
  • 26
    • 0025952925 scopus 로고
    • HIV protease: A novel chemotherapeutic target for AIDS
    • Huff, J.R. HIV protease: a novel chemotherapeutic target for AIDS. J. Med. Chem. 34:2305-2327, 1991.
    • (1991) J. Med. Chem. , vol.34 , pp. 2305-2327
    • Huff, J.R.1
  • 27
    • 0027218692 scopus 로고
    • Structure-based inhibitors of HIV-1 protease
    • Wlodawer, A., Erickson, J.W. Structure-based inhibitors of HIV-1 protease. Annu. Rev. Biochem. 62:543-585, 1993.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 543-585
    • Wlodawer, A.1    Erickson, J.W.2
  • 28
    • 0025108755 scopus 로고
    • Crystallographic analysis of a complex between immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-Å; resolution
    • Fitzgerald, P.M.D., McKeever, B.M., VanMiddlesworth, J.F., et al. Crystallographic analysis of a complex between immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-Å; resolution. J. Biol. Chem. 265:14209-14219, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14209-14219
    • Fitzgerald, P.M.D.1    McKeever, B.M.2    VanMiddlesworth, J.F.3
  • 29
    • 0030973751 scopus 로고    scopus 로고
    • Solution structure of the HIV protease inhibitor acetyl-pepstatin as determined by NMR and molecular modeling
    • Boulanger, Y., Senécal, L., Sauvé, G. Solution structure of the HIV protease inhibitor acetyl-pepstatin as determined by NMR and molecular modeling. J. Biomol. Struct. Dyn. 14:421-428, 1997.
    • (1997) J. Biomol. Struct. Dyn. , vol.14 , pp. 421-428
    • Boulanger, Y.1    Senécal, L.2    Sauvé, G.3
  • 30
    • 0011275132 scopus 로고
    • Direct observation of a ternary complex between the dimeric enzyme HIV-1 protease and a substrate-based inhibitor
    • Baca, M., Kent, S.B.H. Direct observation of a ternary complex between the dimeric enzyme HIV-1 protease and a substrate-based inhibitor. J. Am. Chem. Soc. 114:3992-3993, 1992.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3992-3993
    • Baca, M.1    Kent, S.B.H.2
  • 31
    • 0024344021 scopus 로고
    • Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 Å; resolution
    • Miller, M., Schneider, J., Sathyanarayana, B.K., et al. Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 Å; resolution. Science 246:1149-1152, 1989.
    • (1989) Science , vol.246 , pp. 1149-1152
    • Miller, M.1    Schneider, J.2    Sathyanarayana, B.K.3
  • 32
    • 0029822931 scopus 로고    scopus 로고
    • Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy
    • Wang, Y.-X., Freedberg, D.I., Grzesiek, S., et al. Mapping hydration water molecules in the HIV-1 protease/DMP323 complex in solution by NMR spectroscopy. Biochemistry 35:12694-12704, 1996.
    • (1996) Biochemistry , vol.35 , pp. 12694-12704
    • Wang, Y.-X.1    Freedberg, D.I.2    Grzesiek, S.3
  • 33
    • 0027918556 scopus 로고
    • Water: Now you see it, now you don't
    • Levitt, M., Park, B.H. Water: Now you see it, now you don't. Structure 1:223-226, 1993.
    • (1993) Structure , vol.1 , pp. 223-226
    • Levitt, M.1    Park, B.H.2
  • 34
    • 0027657256 scopus 로고
    • Perspectives - The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry - promise, pitfalls and prognosis
    • Smith, R.D., Light-Wahl, K.J. Perspectives - The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry - promise, pitfalls and prognosis. Biol. Mass Spectrom. 22:493-501, 1993.
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 493-501
    • Smith, R.D.1    Light-Wahl, K.J.2
  • 36
    • 0005211231 scopus 로고    scopus 로고
    • Studying noncovalent protein-RNA interactions and drug binding by electrospray ionization mass spectrometry
    • Ens, W., Standing, K.G., Chernushevich, I.V. (eds.). Dordrecht, The Netherlands: Kluwer
    • Loo, J.A., Sannes-Lowery, K.A., Hu, P., Mack, D.P., Mei, H.-Y. Studying noncovalent protein-RNA interactions and drug binding by electrospray ionization mass spectrometry. In: "New Methods for the Study of Biomolecular Complexes." Ens, W., Standing, K.G., Chernushevich, I.V. (eds.). Dordrecht, The Netherlands: Kluwer, 1998:83-99.
    • (1998) New Methods for the Study of Biomolecular Complexes , pp. 83-99
    • Loo, J.A.1    Sannes-Lowery, K.A.2    Hu, P.3    Mack, D.P.4    Mei, H.-Y.5
  • 38
    • 0029585377 scopus 로고
    • First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses
    • Darlix, J.-L., Lapadat-Tapolsky, M., de Rocquigny, H., Roques, B.P. First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses. J. Mol. Biol. 254:523-537, 1995.
    • (1995) J. Mol. Biol. , vol.254 , pp. 523-537
    • Darlix, J.-L.1    Lapadat-Tapolsky, M.2    De Rocquigny, H.3    Roques, B.P.4
  • 39
    • 0027197020 scopus 로고
    • The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent
    • Gorelick, R.J., Chabot, D.J., Rein, A., Henderson, L.E., Arthur, L.O. The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent. J. Virol. 67:4027-4036, 1993.
    • (1993) J. Virol. , vol.67 , pp. 4027-4036
    • Gorelick, R.J.1    Chabot, D.J.2    Rein, A.3    Henderson, L.E.4    Arthur, L.O.5
  • 40
    • 0029797081 scopus 로고    scopus 로고
    • Biophysical characterization of zinc ejection from HIV nucleocapsid protein by anti-HIV 2,2'dithiobis-[benzamides] and benzisothiazolones
    • Loo, J.A., Holler, T.P., Sanchez, J., Gogliotti, R., Maloney, L., Reily, M.D. Biophysical characterization of zinc ejection from HIV nucleocapsid protein by anti-HIV 2,2'dithiobis-[benzamides] and benzisothiazolones. J. Med. Chem. 39: 4313-4320, 1996.
    • (1996) J. Med. Chem. , vol.39 , pp. 4313-4320
    • Loo, J.A.1    Holler, T.P.2    Sanchez, J.3    Gogliotti, R.4    Maloney, L.5    Reily, M.D.6
  • 41
    • 0026700526 scopus 로고
    • 2+ complex formation analysis with electrospray mass spectrometry
    • 2+ complex formation analysis with electrospray mass spectrometry. FEBS Lett. 311:259-262, 1992.
    • (1992) FEBS Lett. , vol.311 , pp. 259-262
    • Surovoy, A.1    Waidelich, D.2    Jung, G.3
  • 42
    • 0029000952 scopus 로고
    • Specific disulfide formation in the oxidation of HIV-1 zinc finger protein nucleocapsid p7
    • Yu, X.L., Hathout, Y., Fenselau, C., et al. Specific disulfide formation in the oxidation of HIV-1 zinc finger protein nucleocapsid p7. Chem. Res. Toxicol. 8:586-590, 1995.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 586-590
    • Yu, X.L.1    Hathout, Y.2    Fenselau, C.3
  • 43
    • 0030454132 scopus 로고    scopus 로고
    • Characterization of intermediates in the oxidation of zinc fingers in human immunodeficiency virus type 1 nucleocapsid protein P7
    • Hathout, Y., Fabris, D., Han, M.S., Sowder, R.C., II, Henderson, L.E., Fenselau, C. Characterization of intermediates in the oxidation of zinc fingers in human immunodeficiency virus type 1 nucleocapsid protein P7. Drug Metab. Dispos. 24:1395-1400, 1996.
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 1395-1400
    • Hathout, Y.1    Fabris, D.2    Han, M.S.3    Sowder II, R.C.4    Henderson, L.E.5    Fenselau, C.6
  • 44
    • 0030457336 scopus 로고    scopus 로고
    • Retention of thiol protons in two classes of protein zinc ion coordination centers
    • Fabris, D., Zaia, J., Hathout, Y., Fenselau, C. Retention of thiol protons in two classes of protein zinc ion coordination centers. J. Am. Chem. Soc. 118:12242-12243, 1996.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12242-12243
    • Fabris, D.1    Zaia, J.2    Hathout, Y.3    Fenselau, C.4
  • 45
    • 0029876943 scopus 로고    scopus 로고
    • Zinc binding to the HIV-1 nucleocapsid protein: A thermodynamic investigation by fluorescence spectroscopy
    • Mély, Y., de Rocquigny, H., Morellet, N., Roques, B.P., Gérard, D. Zinc binding to the HIV-1 nucleocapsid protein: a thermodynamic investigation by fluorescence spectroscopy. Biochemistry 35:5175-5182, 1996.
    • (1996) Biochemistry , vol.35 , pp. 5175-5182
    • Mély, Y.1    De Rocquigny, H.2    Morellet, N.3    Roques, B.P.4    Gérard, D.5
  • 46
    • 0027325412 scopus 로고
    • Identification of a binding site for the human immunodeficiency virus type 1 nucleocapsid protein
    • Sakaguchi, K., Zambrano, N., Baldwin, E.T., et al. Identification of a binding site for the human immunodeficiency virus type 1 nucleocapsid protein. Proc. Natl. Acad. Sci. USA 90:5219-5223, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5219-5223
    • Sakaguchi, K.1    Zambrano, N.2    Baldwin, E.T.3
  • 47
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 ψ-RNA recognition element
    • De Guzman, R.N., Wu, Z.R., Stalling, C.C., Pappalardo, L., Borer, P.N., Summers, M.F. Structure of the HIV-1 nucleocapsid protein bound to the SL3 ψ-RNA recognition element. Science 279:384-388, 1998.
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 49
    • 0031213609 scopus 로고    scopus 로고
    • Investigation of calcium-induced, noncovalent association of calmodulin with melittin by electrospray ionization mass spectrometry
    • Nemirovskiy, O.V., Ramanathan, R., Gross, M.L. Investigation of calcium-induced, noncovalent association of calmodulin with melittin by electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 8:809-812, 1997.
    • (1997) J. Am. Soc. Mass Spectrom. , vol.8 , pp. 809-812
    • Nemirovskiy, O.V.1    Ramanathan, R.2    Gross, M.L.3
  • 50
    • 0028928486 scopus 로고
    • Biomolecular folding in vacuo!!!(?)
    • Wolynes, P.G. Biomolecular folding in vacuo!!!(?). Proc. Natl. Acad. Sci. USA 92:2426-2427, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2426-2427
    • Wolynes, P.G.1
  • 51
    • 0001221850 scopus 로고    scopus 로고
    • Higher order structure in the gas phase reflects solution structure
    • Loo, J.A., He, J.-X., Cody, W.L. Higher order structure in the gas phase reflects solution structure. J. Am. Chem. Soc. 120:4542-4543, 1998.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4542-4543
    • Loo, J.A.1    He, J.-X.2    Cody, W.L.3


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