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  • Arantes, E.C., Prado, W.A., Sampaio, S.V., and Giglio, J.R. 1989. A simplified procedure for the fractionation of Tityus serrulatus venom: Isolation and partial characterization of TsTX-IV, a new neurotoxin. Toxicon 27: 907916.
  • Ashcroft, F.M. 2000. Ion channels and disease. Academic Press, London.
  • Batista, C.V.F., Gomez-Lagunas, F., Rodriguez de la Vega, R.C., Hajdu, P., Panyi, G., Gaspar, R., and Possani, L.D. 2002. Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K+-channels with distinctly different affinities. Biochim. Biophys. Acta 1601: 123131.
  • Bauer, F., Schweimer, K., Kluver, E., Conejo-Garcia, J.R., Forssmann, W.G., Rosch, P., Adermann, K., and Sticht, H. 2001. Structure determination of human and murine β-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci. 10: 24702479.
  • Bax, A. and Davis, D.G. 1985. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65: 355360.
  • Berendsen, H.J.C., Postma, J.P.M., van Gunsteren, W.F., and Hermans, J. 1981. Interaction models for water in relation to protein hydration. In Intermolecular forces (ed. B.Pullman), pp. 331342. D. Reidel Publishing Co., Dordrecht, The Netherlands.
  • Bloch, C. Jr., Patel, S.U., Baud, F., Zvelebil, M.J., Carr, M.D., Sadler, P.J., and Thornton, J.M. 1998. 1H NMR structure of an antifungal γ-thionin protein SIα1: Similarity to scorpion toxins. Proteins 15: 334349.
  • Bontems, F., Roumestand, C., Boyot, P., Gilquim, B., Doljansky, Y., Menez, A., and Toma, F. 1991. Three-dimensional structure of natural charybdotoxyn in aqueous solution by 1H-NMR. Charybdotoxyn possesses a structural motif found in other scorpion toxins. Eur. J. Biochem. 196: 1928.
  • Canto, J., Fernandez, Y., Pons, M., Giralt, M., and Perez, J.J. 1999. Molecular dynamics study of Kaliotoxin in water. J. Biol. Macromol. 24: 19.
  • Cheatham, T.E. III, Miller, J.L., Fox, T., Darden, T.A., and Kollman, P.A. 1995. Molecular dynamics simulations on solvated biomolecular systems: The Particle Mesh Ewald method leads to stable trajectories of DNA, RNA, and proteins. J. Amer. Chem. Soc. 117: 41934194.
  • Cohen, L., Karbat, I., Gilles, N., Froy, O., Corzo, G., Angelovici, R., Gordon, D., and Gurevitz, M. 2004. Dissection of the functional surface of an anti-insect excitatory toxin illuminates a putative “hot spot” common to all scorpion β-toxins affecting Na+ channels. J. Biol. Chem. 279: 82068211.
  • Corona, M., Gurrola, G.B., Merino, E., Cassulini, R.R., Valdez-Cruz, N.A., García, B., Ramírez-Domínguez, M.E., Coronas, F.I.V., Zamudio, F.Z., Wanke, E., et al. 2002. A large number of novel Ergtoxin-like genes and ERG K+-channels blocking peptides from scorpions of the genus Centruroides. FEBS Lett. 532: 121126.
  • Coronas, F.V., de Roodt, A.R., Olamendi-Portugal, T., Zamudio, F.Z., Batista, C.V.F., Gomez-Lagunas, F., and Possani, L.D. 2003. Disulfide bridges and blockage of Shaker B K+-channels by another butantoxin peptide purified from the Argentinean scorpion Tityus trivittatus. Toxicon 41: 173179.
  • Darden, T., York, D., and Pedersen, L. 1993. Particle Mesh Ewald: An N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 98: 1008910092.
  • Dauber-Osguthorpe, P., Roberts, P., Osguthorpe, V.A., Wolff, D.J., Genest, M., and Hagler, A.T. 1988. Structure and energetics of ligand binding to proteins: E. coli dihydropholate reductase-tremethoprim, a drug-receptor system. Proteins 4: 3147.
  • Davis, D.G. and Bax, A. 1985. Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107: 28202821.
  • Dyke, T.R., Duggan, B.M., Pennington, M.W., Byrnes, M.E., Kem, W.R., and Norton, R.S. 1996. Synthesis and structural characterization of analogues of the potassium channel blocker charybdotoxin. Biochim. Biophys. Acta 1292: 3138.
  • Ellis, K.C., Tenenholz, T.C., Jerng, H., Hayhurst, M., Dudlak, C.S., Gilly, W.F., Blaustein, M.P., and Weber, D.J. 2001. Interaction of a toxin from the scorpion Tityus serrulatus with a cloned K+ channel from squid (sqKv1A). Biochemistry 40: 59425953.
  • Everhart, D., Cartier, E.G., Malhotra, A., Gomes, A.V., McIntosh, J.M., and Luetje, C.W. 2004. Determinants of potency on a β-conotoxin MII, a peptide antagonist of neuronal nicotinic receptors. Biochemistry 43: 27322737.
  • Fant, F., Vranken, W., Brekaert, W., and Borremans, F. 1998. Determination of the three-dimensional solution structure of Raphanus sativus antifungal protein 1 by 1H NMR. J. Mol. Biol. 279: 257270.
  • Fernández, I., Romi, R., Szendeffy, S., Martin-Eauclaire, M.F., Rochat, H., Van Rietschoten, J., Pons, M., and Giralt, E. 1994. Kaliotoxin (1–37) shows structural differences with related potassium channel blockers. Biochemistry 33: 1425614263.
  • Fersht, A. 1998. Structure and mechanism in protein science. W.H. Freeman and Co., New York.
  • Frémont, V., Blanc, E., Crest, M., Martin-Eauclaire, M., Gola, M., Darbon, H., and van Rietschoten, J. 1997. Dipole moments of scorpion toxins direct the interaction towards small- or large-conductance Ca+2-activated K+ channels. Lett. Pept. Sci. 4: 305312.
  • Gairí, M., Romi, R., Fernandez, I., Rochat, H., Martin-Eauclaire, M.F., Van Rietschoten, J., Pons, M., and Giralt, E. 1997. 3D Structure of Kaliotoxin: Is residue 34 a key for channel selectivity? J. Pept. Sci. 3: 314319.
  • Garcia, M.L., Gao, Y.D., McManus, O.B., and Kaczorowski, G.J. 2001. Potassium channels: From scorpion venoms to high-resolution structure. Toxicon 39: 739748.
  • Gnanakaran, S., Nymeyer, H., Portman, J., Sanbonmatsu, K.Y., and Garcia, A.E. 2003. Peptide folding simulations. Curr. Opin. Struct. Biol. 13: 168174.
  • Goudet, C., Chi, C.W., and Tytgat, J. 2002. An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch. Toxicon 40: 12391258.
  • Griesinger, C., Otting, G., Wüthrich, K., and Ernst, R.R. 1988. Clean TOCSY for 1H spin-system identification in macromolecules. J. Am. Chem. Soc. 110: 78707872.
  • Grottesi, A. and Sansom, M.S.P. 2003. Molecular dynamics simulation of a K+ channel blocker: Tc1 toxin from Tityus cambridgei. FEBS Lett. 535: 2933.
  • Güntert, P., Braun, W., and Wüthrich, K. 1991. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217: 517530.
  • Güntert, P., Mumenthaler, C., and Wüthrich, K. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273: 283298.
  • Hess, B., Bekker, H., Berendsen, H.J.C., and Fraaije, J.G.E.M. 1997. LINCS: A linear constraint solver for molecular simulations. J. Comp. Chem. 18: 14631472.
  • Holaday, S.K. Jr., Martin, B.M., Fletcher, P.L. Jr., and Krishna, N.R. 2000. NMR solution structure of butantoxin. Arch. Biochem. Biophys. 379: 1827.
  • Hu, H., Clarkson, M.W., Hermans, J., and Lee, A.L. 2003. Increased rigidity of eglin c at acidic pH: Evidence from NMR spin relaxation and MD simulations. Biochemistry 42: 1385613868.
  • Kipping, M., Zarnt, T., Steffen, K., Reimer, U., Fischer, G., and Bayer, P. 2001. Increased backbone flexibility in threonine45-phosphorylated hirudin upon pH change. Biochemistry 40: 79577963.
  • Krezel, A.M., Kasibhatla, C., Hidalgo, P., MacKinnon, R., and Wagner, G. 1995. Solution structure of the potassium channel inhibitor agitoxin 2: Caliper for probing channel geometry. Protein Sci. 4: 14781489.
  • Kumar, A., Ernst, R.R., and Wüthrich, K. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95: 16.
  • Laskowski, R.A., Rullmann, J.A., MacArthur, M.W., Kaptein, R., and Thornton, J.M. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8: 477486.
  • Lindahl, E., Hess, B., and van der Spoel, D. 2001. Gromacs 3.0: A package for molecular simulation and trajectory analysis. J. Mol. Mod. 7: 306317.
  • Meunier, S., Bernassau, J.-M., Sabastier, M.F., Martin-Eauclaire, M.F., van Rietschoten, J., Cambillau, C., and Darbon, H. 1993. Solution structure of P05-NH2, a scorpion toxin analog with high affinity for apamin-sensitive potassium channels. Biochemistry 32: 1196911976.
  • Miyamoto, S. and Kollman, P.A. 1992. SETTLE: An analytical version of the SHAKE and RATTLE algorithm for rigid water models. J. Comp. Chem. 13: 952962.
  • Novello, J.C., Arantes, E.C., Varanda, W.A., Oliveira, B., Giglio, J.R., and Marangoni, S. 1999. TsTX-IV, a short chain four-disulfide-bridged neurotoxin from Tityus serrulatus venom which acts on Ca2+-activated K+ channels. Toxicon 37: 651660.
  • Pimenta, A.M.C., Mansuelle, P., Diniz, C.R., and Martin-Eauclaire, M.F. 2003. Covalent structure and some pharmacological features of native and cleaved α-KTx12.1, a four disulfide-bridged toxin from Tityus serrulatus venom. J. Pept. Sci. 9: 132140.
  • Piotto, M., Saudek, V., and Sklenár, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2: 661665.
  • Pristovšek, P., Lücke, C., Reincke, B., Ludwig, B., and Rüterjans, H. 2000. Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state. Eur. J. Biochem. 267: 42054212.
  • Rance, M., Sørensen, O.W., Bodenhausen, G., Wagner, G., Ernst, R.R., and Wüthrich, K. 1983. Improved spectral resolution in COSY 1H NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Commun. 117: 479485.
  • Rodriguez de la Vega, R.C., Merino, E., Becerril, B., and Possani, L.D. 2003. Novel interactions between K+ channels and scorpion toxins. Trends Pharmacol. Sci. 24: 222227.
  • Sawai, M.V., Jia, P.H., Liu, L., Aseyev, V., Wiencek, J.M., McCray, P.B. Jr., Ganz, T., Kearney, W.R., and Tack, B.F. 2001. The NMR structure of human β-defensin-2 reveals a novel α-helical segment. Biochemistry 40: 38103816.
  • Sforça, M.L., Oyama, S. Jr., Canduri, F., Lorenzi, C.C.B., Pertinhez, T.A., Konno, K., Souza, M.B, Palma, M.S., Neto, J.R., Azevedo, W.F. Jr., et al. 2004. How C-terminal carboxyamidation alters the biological activity of peptides from the venom of the eumenine solitary wasp. Biochemistry 43: 56085617.
  • Shieh, C.C., Coghlan, M., Sullivan, J.P., and Gopalakrishnan, M. 2000. Potassium channels: Molecular defects, diseases, and therapeutic opportunities. Pharmacol. Rev. 52: 557593.
  • Steen, K.H., Steen, A.E., Kreysel, H-W., and Reeh, P.W. 1996. Inflammatory mediators potentiate pain induced by experimental tissue acidosis. Pain 66: 163170.
  • Tenenholz, T.C., Klenk, K.C., Matteson, D.R., Blaustein, M.P., and Weber, D.J. 2000. Structural determinants of scorpion affinity: The charybdotoxin (α-KTX) family of K+-channel blocking peptides. Rev. Physiol. Biochem. Pharmacol. 140: 135185.
  • Thompson, J. and Begenisich, T. 2000. Electrostatic interaction between charybdotoxin and a tetrameric mutant of Shaker K+ channels. Biophys. J. 78: 23822391.
  • Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 46734680.
  • Tytgat, J., Chandy, K.G., Garcia, M.L., Gutman, G.A., Martin-Eauclaire, M.F., van der Walt, J.J., and Possani, L.D. 1999. A unified nomenclature for short-chain peptides isolated from scorpion venoms: α-KTx molecular subfamilies. Trends Pharmacol. Sci. 20: 444447.
  • van Aalten, D.M.F., de Groot, B.L., Findlay, J.B.C., Berendsen, H.J.C., and Amadei, A. 1996. A comparison of techniques for calculating protein essential dynamics. J. Comp. Chem. 18: 169181.
  • Waldmann, R. and Lasdunski, M. 1998. H+-gated cation channels: Neuronal acid sensors in the NaC/DEG family of ion channels. Curr. Opin. Neurol. 8: 418424.
  • Wang, I., Wu, S.-H., Chang, H.-K., Shieh, R.-C., Yu, H.-M., and Chen, C. 2002. Solution structure of a K+-channel blocker from the scorpion Tityus cambridgei. Protein Sci. 11: 390400.
  • Wishart, D.S., Sykes, B.D., and Richards, F.M. 1992. The Chemical Shift Index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31: 16471651.
  • Wu, X. and Brooks, B.R. 2004. β-Hairpin folding mechanism of a nine-residue peptide revealed from molecular dynamics simulations in explicit water. Biophys. J. 86: 19461958.
  • Wüthrich, K. 1986. NMR of proteins and nucleic acids. Wiley Interscience, New York.