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Volumn 5, Issue 4, 1997, Pages 571-583

Solution structure of the sodium channel antagonist conotoxin GS: A new molecular caliper for probing sodium channel geometry

Author keywords

cis peptide bond; NMR spectroscopy; carboxyglutamic acid; trans hydroxyproline; conotoxin

Indexed keywords

ANIMALIA; CONUS GEOGRAPHUS; GASTROPODA; MOLLUSCA;

EID: 0031569801     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00212-8     Document Type: Article
Times cited : (49)

References (58)
  • 1
    • 0023161082 scopus 로고
    • An integrated view of the molecular toxinology of sodium channel gating in excitable cells
    • Strichartz, G., Rando, T. & Wang, G.K. (1987). An integrated view of the molecular toxinology of sodium channel gating in excitable cells. Annu. Rev. Neurosci. 10, 237-267.
    • (1987) Annu. Rev. Neurosci. , vol.10 , pp. 237-267
    • Strichartz, G.1    Rando, T.2    Wang, G.K.3
  • 2
    • 0024280869 scopus 로고
    • Structure and function of voltage-sensitive ion channels
    • Catterall, W.A. (1988). Structure and function of voltage-sensitive ion channels. Science 242, 50-61.
    • (1988) Science , vol.242 , pp. 50-61
    • Catterall, W.A.1
  • 3
    • 0024811092 scopus 로고
    • A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II
    • Noda, M., Suzuki, H., Numa, S. & Stühmer, W. (1989). A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II. FEBS Lett. 259, 213-216.
    • (1989) FEBS Lett. , vol.259 , pp. 213-216
    • Noda, M.1    Suzuki, H.2    Numa, S.3    Stühmer, W.4
  • 4
    • 0026072218 scopus 로고
    • Mapping the site of block, by tetrodotoxin and saxitoxin of sodium channel II
    • Terlau, H., et al., & Numa, S. (1991). Mapping the site of block, by tetrodotoxin and saxitoxin of sodium channel II. FEBS Lett. 293, 93-96.
    • (1991) FEBS Lett. , vol.293 , pp. 93-96
    • Terlau, H.1    Numa, S.2
  • 5
    • 0028180093 scopus 로고
    • The μl skeletal muscle sodium channel: Mutation E403Q eliminates sensitivity to tetrodotoxin but not to μ-conotoxins GIIIA and GIIIB
    • Stephan, M.M., Potts, J.F. & Agnew, W.S. (1994). The μl skeletal muscle sodium channel: mutation E403Q eliminates sensitivity to tetrodotoxin but not to μ-conotoxins GIIIA and GIIIB. J. Membr. Biol. 137, 1-8.
    • (1994) J. Membr. Biol. , vol.137 , pp. 1-8
    • Stephan, M.M.1    Potts, J.F.2    Agnew, W.S.3
  • 7
    • 0028970541 scopus 로고
    • + channel mutant: Possible localisation of a binding site at the outer vestibule
    • + channel mutant: possible localisation of a binding site at the outer vestibule. Biophys. J. 69, 1657-1665.
    • (1995) Biophys. J. , vol.69 , pp. 1657-1665
    • Dudley, S.C.1    Todt, H.2    Lipkind, G.3    Fozzard, H.A.4
  • 8
    • 0029417234 scopus 로고
    • Characterising the μ-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations
    • Chahine, M., et al., & Kallen, R.G. (1995). Characterising the μ-conotoxin binding site on voltage-sensitive sodium channels with toxin analogs and channel mutations. Recept. Channels 3, 161-174.
    • (1995) Recept. Channels , vol.3 , pp. 161-174
    • Chahine, M.1    Kallen, R.G.2
  • 9
    • 0021097539 scopus 로고
    • The amino acid sequences of homologous hydroxyproline-containing myotoxins from the marine snail Conus geographus venom
    • Sato, S., Nakamura, H., Ohizumi, Y., Kobayashi, J. & Hirata, Y. (1983). The amino acid sequences of homologous hydroxyproline-containing myotoxins from the marine snail Conus geographus venom. FEBS Lett. 155, 277-280.
    • (1983) FEBS Lett. , vol.155 , pp. 277-280
    • Sato, S.1    Nakamura, H.2    Ohizumi, Y.3    Kobayashi, J.4    Hirata, Y.5
  • 10
    • 0022359989 scopus 로고
    • Conus geographus toxins that discriminate between neuronal and muscle sodium channels
    • Cruz, L.J., et al., & Moczydlowski, E. (1985). Conus geographus toxins that discriminate between neuronal and muscle sodium channels. J. Biol. Chem. 260, 9280-9288.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9280-9288
    • Cruz, L.J.1    Moczydlowski, E.2
  • 11
    • 0023711980 scopus 로고
    • A novel sodium channel inhibitor from Conus geographus: Purification, structure, and pharmacological properties
    • Yanagawa, Y., Abe, T., Satake, M., Odani, S., Suzuki, J. & Ishikawa, K. (1988). A novel sodium channel inhibitor from Conus geographus: purification, structure, and pharmacological properties. Biochemistry 27, 6256-6262.
    • (1988) Biochemistry , vol.27 , pp. 6256-6262
    • Yanagawa, Y.1    Abe, T.2    Satake, M.3    Odani, S.4    Suzuki, J.5    Ishikawa, K.6
  • 13
    • 0022931513 scopus 로고
    • 3H]saxitoxin binding to skeletal muscle sodium channels by geographutoxin II, a polypeptide channel blocker
    • 3H]saxitoxin binding to skeletal muscle sodium channels by geographutoxin II, a polypeptide channel blocker. J. Biol. Chem. 261, 6149-6152.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6149-6152
    • Ohizumi, Y.1    Nakamura, H.2    Kobayashi, J.3    Catterall, W.A.4
  • 14
    • 0026760836 scopus 로고
    • Chimeric study of sodium channels from rat skeletal and cardiac muscle
    • Chen, L.-Q., Chahine, M., Kallen, R.G., Barchi, R.L. & Horn, R. (1992). Chimeric study of sodium channels from rat skeletal and cardiac muscle. FEBS Lett. 309, 253-257.
    • (1992) FEBS Lett. , vol.309 , pp. 253-257
    • Chen, L.-Q.1    Chahine, M.2    Kallen, R.G.3    Barchi, R.L.4    Horn, R.5
  • 15
    • 0342923750 scopus 로고
    • Synthesis and disulfide structure determination of conotoxin GS, a γ-carboxyglutamic acid-containing neurotoxic peptide
    • Nakao, M., Nishiuchi, Y., Nakata, M., Watanabe, T.X., Kimura, T. & Sakakibara, S. (1995). Synthesis and disulfide structure determination of conotoxin GS, a γ-carboxyglutamic acid-containing neurotoxic peptide. Letters in Peptide Science 2, 17-26.
    • (1995) Letters in Peptide Science , vol.2 , pp. 17-26
    • Nakao, M.1    Nishiuchi, Y.2    Nakata, M.3    Watanabe, T.X.4    Kimura, T.5    Sakakibara, S.6
  • 16
    • 0025788864 scopus 로고
    • Tertiary structure of conotoxin GIIIA in aqueous solution
    • Lancelin, J.-M., et al., & Inagaki, F. (1991). Tertiary structure of conotoxin GIIIA in aqueous solution. Biochemistry 30, 6908-6916.
    • (1991) Biochemistry , vol.30 , pp. 6908-6916
    • Lancelin, J.-M.1    Inagaki, F.2
  • 17
    • 0025960783 scopus 로고
    • Solution structure of μ-conotoxin GIIIA analysed by 2D-NMR and distance geometry calculations
    • Ott, K.-H., Becker, S., Gordon, R.D. & Rüterjans, H. (1991). Solution structure of μ-conotoxin GIIIA analysed by 2D-NMR and distance geometry calculations. FEBS Lett. 278, 160-166.
    • (1991) FEBS Lett. , vol.278 , pp. 160-166
    • Ott, K.-H.1    Becker, S.2    Gordon, R.D.3    Rüterjans, H.4
  • 18
    • 0027078665 scopus 로고
    • Structure-activity relationships of μ-conotoxin GIIIA: Structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations
    • Wakamatsu, K., et al., & Sato, K. (1992). Structure-activity relationships of μ-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Biochemistry 31, 12577-12584.
    • (1992) Biochemistry , vol.31 , pp. 12577-12584
    • Wakamatsu, K.1    Sato, K.2
  • 19
    • 0030016085 scopus 로고    scopus 로고
    • Three-dimensional solution structure of μ-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels
    • Hill, J.M., Alewood, P.F. & Craik, D.J. (1996). Three-dimensional solution structure of μ-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels. Biochemistry 35, 8824-8835.
    • (1996) Biochemistry , vol.35 , pp. 8824-8835
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 20
    • 0001021863 scopus 로고
    • Conus peptides as chemical probes for receptors and ion channels
    • Myers, R.A., Cruz, L.J., Rivier, J.E. & Olivera, B.M. (1993). Conus peptides as chemical probes for receptors and ion channels. Chem. Rev. 93, 1923-1936.
    • (1993) Chem. Rev. , vol.93 , pp. 1923-1936
    • Myers, R.A.1    Cruz, L.J.2    Rivier, J.E.3    Olivera, B.M.4
  • 21
    • 0030449042 scopus 로고    scopus 로고
    • Calcium binding properties of synthetic γ-carboxyglutamic acid-containing marine cone snail 'sleeper' peptides, conantokin-G and conantokin-T
    • Prorok, M., Warder, S.E., Blandl, T. & Castellino, F.J. (1996). Calcium binding properties of synthetic γ-carboxyglutamic acid-containing marine cone snail 'sleeper' peptides, conantokin-G and conantokin-T. Biochemistry 35, 16528-16534.
    • (1996) Biochemistry , vol.35 , pp. 16528-16534
    • Prorok, M.1    Warder, S.E.2    Blandl, T.3    Castellino, F.J.4
  • 22
    • 0031035377 scopus 로고    scopus 로고
    • Determination of the solution structures of conantokin-G and conantokin-T by CD and NMR spectroscopy
    • Skjaerbaek, N., Nielsen, K.J., Lewis, R.J., Alewood, P. & Craik, D.J. (1997). Determination of the solution structures of conantokin-G and conantokin-T by CD and NMR spectroscopy. J. Biol. Chem. 272, 2291-2299.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2291-2299
    • Skjaerbaek, N.1    Nielsen, K.J.2    Lewis, R.J.3    Alewood, P.4    Craik, D.J.5
  • 23
    • 0029985569 scopus 로고    scopus 로고
    • Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with γ-carboxyglutamic acid, from the sea snail, Conus textile
    • Nakamura, T., Yu, Z., Fainzilber, M. & Burlingame, A.L. (1996). Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with γ-carboxyglutamic acid, from the sea snail, Conus textile. Protein Sci. 5, 524-530.
    • (1996) Protein Sci. , vol.5 , pp. 524-530
    • Nakamura, T.1    Yu, Z.2    Fainzilber, M.3    Burlingame, A.L.4
  • 25
    • 0000936646 scopus 로고
    • 13C-NMR spectra of two different molecular conformations of a cyclic pentapeptide
    • 13C-NMR spectra of two different molecular conformations of a cyclic pentapeptide. FEBS Lett. 25, 104-108.
    • (1972) FEBS Lett. , vol.25 , pp. 104-108
    • Wüthrich, K.1    Tun-kyi, A.2    Schwyzer, R.3
  • 27
    • 0025553059 scopus 로고
    • NMR investigations of protein structure
    • Wagner, G. (1990) NMR investigations of protein structure. Prog. NMR Spectrosc. 22, 101-139.
    • (1990) Prog. NMR Spectrosc. , vol.22 , pp. 101-139
    • Wagner, G.1
  • 28
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D.S., Sykes, B.D. & Richards, P.M. (1992). The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, P.M.3
  • 29
    • 0027236599 scopus 로고
    • Determination of the disulfide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data
    • Klaus, W., Broger, C., Gerber, P. & Senn, H. (1993). Determination of the disulfide bonding pattern in proteins by local and global analysis of nuclear magnetic resonance data. J. Mol. Biol. 232, 897-906.
    • (1993) J. Mol. Biol. , vol.232 , pp. 897-906
    • Klaus, W.1    Broger, C.2    Gerber, P.3    Senn, H.4
  • 30
    • 0029885431 scopus 로고    scopus 로고
    • Primary structural motifs of Conus peptides
    • Singh, B.R. & Tu, A.T., eds, Plenum Press, New York
    • Cruz, L.J. (1996). Primary structural motifs of Conus peptides. In Natural Toxins II. (Singh, B.R. & Tu, A.T., eds), pp. 155-167, Plenum Press, New York.
    • (1996) Natural Toxins II , pp. 155-167
    • Cruz, L.J.1
  • 31
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF: A program to identify and analyse structural motifs in proteins
    • Hutchinson, E.G. & Thornton, J.M. (1996). PROMOTIF: a program to identify and analyse structural motifs in proteins. Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 33
    • 0025113022 scopus 로고
    • β-Turns and their distortions: A proposed new nomenclature
    • Wilmot, C.M. & Thornton, J.M. (1990). β-Turns and their distortions: a proposed new nomenclature. Protein Eng. 3, 479-493.
    • (1990) Protein Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thornton, J.M.2
  • 34
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β sheet in toxic and inhibitory polypeptides
    • Pallaghy, P.K., Nielsen, K.J., Craik, D.J. & Norton, R.S. (1994). A common structural motif incorporating a cystine knot and a triple-stranded β sheet in toxic and inhibitory polypeptides. Protein Sci. 3, 1833-1839.
    • (1994) Protein Sci. , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 35
    • 0025299887 scopus 로고
    • Occurrence and role of cis peptide bonds in protein structures
    • Stewart, D.E., Sarkar, A. & Wampler, J.E. (1990). Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214, 253-260.
    • (1990) J. Mol. Biol. , vol.214 , pp. 253-260
    • Stewart, D.E.1    Sarkar, A.2    Wampler, J.E.3
  • 36
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur, M.W. & Thornton, J.M. (1991). Influence of proline residues on protein conformation. J. Mol. Biol. 218, 397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 37
    • 0025955695 scopus 로고
    • Active site of μ-conotoxin GIIIA, a peptide blocker of muscle sodium channels
    • Sato, K., et al., & Inagaki, F. (1991). Active site of μ-conotoxin GIIIA, a peptide blocker of muscle sodium channels. J. Biol. Chem. 266, 16989-16991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16989-16991
    • Sato, K.1    Inagaki, F.2
  • 38
    • 0026657359 scopus 로고
    • Action of derivatives of μ-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates
    • Becker, S., Prusak-Sochaczewski, E., Zamponi, G., Beck-Sickinger, A.G., Gordon, R.G. & French, R.J. (1992). Action of derivatives of μ-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry 31, 8229-8238.
    • (1992) Biochemistry , vol.31 , pp. 8229-8238
    • Becker, S.1    Prusak-Sochaczewski, E.2    Zamponi, G.3    Beck-Sickinger, A.G.4    Gordon, R.G.5    French, R.J.6
  • 39
    • 0029243371 scopus 로고
    • The solution structure of ω-Agatoxin-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta
    • Reily, M.D., Thanabal, V. & Adams, M.E. (1995). The solution structure of ω-Agatoxin-IVB, a P-type calcium channel antagonist from venom of the funnel web spider, Agelenopsis aperta. J. Biomol. NMR 5, 122-132.
    • (1995) J. Biomol. NMR , vol.5 , pp. 122-132
    • Reily, M.D.1    Thanabal, V.2    Adams, M.E.3
  • 40
    • 0029084407 scopus 로고
    • Three-dimensional solution structure of the calcium channel antagonist ω-agatoxin IVA: Consensus molecular folding of calcium channel blockers
    • Kim, J.I., et al., & Arata, Y. (1995). Three-dimensional solution structure of the calcium channel antagonist ω-agatoxin IVA: consensus molecular folding of calcium channel blockers. J. Mol. Biol. 250, 659-671.
    • (1995) J. Mol. Biol. , vol.250 , pp. 659-671
    • Kim, J.I.1    Arata, Y.2
  • 41
    • 0029767552 scopus 로고    scopus 로고
    • Strategy for rapid immobilisation of prey by a fish-hunting marine snail
    • Terlau, H., Shon, K.-J., Grilley, M., Stocker, M., Stühmer, W. & Olivera, B.M. (1996). Strategy for rapid immobilisation of prey by a fish-hunting marine snail. Nature 381, 148-151.
    • (1996) Nature , vol.381 , pp. 148-151
    • Terlau, H.1    Shon, K.-J.2    Grilley, M.3    Stocker, M.4    Stühmer, W.5    Olivera, B.M.6
  • 42
    • 0028695949 scopus 로고
    • Snail and spider toxins share a similar tertiary structure and 'cysteine motif'
    • Narasimhan, L., Singh, J., Humblet, C., Guruprasad, K. & Blundell, T. (1994). Snail and spider toxins share a similar tertiary structure and 'cysteine motif'. Nat. Struct. Biol. 1, 850-852.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 850-852
    • Narasimhan, L.1    Singh, J.2    Humblet, C.3    Guruprasad, K.4    Blundell, T.5
  • 43
    • 0027205407 scopus 로고
    • Solution structure of ω-conotoxin GVIA using 2D NMR spectroscopy and relaxation matrix analysis
    • Davis, J.H., Bradley, E.K., Miljanich, G.P., Nadasdi, L., Ramachandran, J. & Basus, V.J. (1993). Solution structure of ω-conotoxin GVIA using 2D NMR spectroscopy and relaxation matrix analysis. Biochemistry 32, 7396-7405.
    • (1993) Biochemistry , vol.32 , pp. 7396-7405
    • Davis, J.H.1    Bradley, E.K.2    Miljanich, G.P.3    Nadasdi, L.4    Ramachandran, J.5    Basus, V.J.6
  • 44
    • 0027379001 scopus 로고
    • Three-dimensional structure in solution of the calcium channel blocker ω-conotoxin
    • Pallaghy, P.K., Duggan B.M., Pennington, M.W. & Norton, R.S. (1993). Three-dimensional structure in solution of the calcium channel blocker ω-conotoxin. J. Mol. Biol. 234, 405-420.
    • (1993) J. Mol. Biol. , vol.234 , pp. 405-420
    • Pallaghy, P.K.1    Duggan, B.M.2    Pennington, M.W.3    Norton, R.S.4
  • 46
    • 0027517346 scopus 로고
    • Solution structure of the calcium channel antagonist ω-conotoxin GVIA
    • Skalicky, J.J., Metzler, W.J., Ciesla, D.J., Galdes, A. & Pardi, A. (1993), Solution structure of the calcium channel antagonist ω-conotoxin GVIA. Protein Sci. 2, 1591-1603.
    • (1993) Protein Sci. , vol.2 , pp. 1591-1603
    • Skalicky, J.J.1    Metzler, W.J.2    Ciesla, D.J.3    Galdes, A.4    Pardi, A.5
  • 47
    • 0029986992 scopus 로고    scopus 로고
    • Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities
    • Omecinsky, D.O., Holub, K.E., Adams, M.E. & Reily, M.D. (1996). Three-dimensional structure analysis of μ-agatoxins: further evidence for common motifs among neurotoxins with diverse ion channel specificities. Biochemistry 35, 2836-2844.
    • (1996) Biochemistry , vol.35 , pp. 2836-2844
    • Omecinsky, D.O.1    Holub, K.E.2    Adams, M.E.3    Reily, M.D.4
  • 51
    • 33644757144 scopus 로고
    • Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
    • Bax, A., Griffey, R.H. & Hawkins, B.L. (1983). Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Reson. 55, 301-315.
    • (1983) J. Magn. Reson. , vol.55 , pp. 301-315
    • Bax, A.1    Griffey, R.H.2    Hawkins, B.L.3
  • 52
    • 0002532387 scopus 로고
    • Sensitivity-enhanced two-dimensional heteronuclear relayed coherence transfer NMR spectroscopy
    • Lerner, L. & Bax, A. (1986). Sensitivity-enhanced two-dimensional heteronuclear relayed coherence transfer NMR spectroscopy. J. Magn. Reson. 69, 375-380.
    • (1986) J. Magn. Reson. , vol.69 , pp. 375-380
    • Lerner, L.1    Bax, A.2
  • 54
    • 0023998438 scopus 로고
    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
    • Nilges, M., Gronenborn, A.M., Brünger, A.T. & Clore, G.M. (1988). Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27-38.
    • (1988) Protein Eng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brünger, A.T.3    Clore, G.M.4
  • 56
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structure coordinates
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structure coordinates. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 57
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 58
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.1


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