Abstract
The resonant recognition model is used to predict structurally and functionally important amino acid residues (so-called hot spots) in the neuropeptide Y (NPY) family. Thirty-three polypeptides belong to this family. All of them consist of 36 amino acids. The model predicts that residues 10 and 28 in the polypeptides are hot spots. In the 33 polypeptides, most of the amino acids at residue 10 are acidic amino acids, glutamic acid and aspartic acid. Other minor amino acids, serine, glycine, and proline, have high probabilities of β-turn occurrence. Amino acids at residue 28 are all branched hydrophobic amino acids, isoleucine, leucine, and valine. The profile for predicting hot spots indicates repeating patterns of residues 1–18 and residues 19–36. Absolute values at residue i and residue i + 18 are the same, but these residues have opposite signs. Therefore the model of the NPY family predicts hot spots concerning a combination of residue i and residue i + 18.
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REFERENCES
Allen, J., Novotny, J., Martin, J., and Heinrich, G. (1987). Proc. Natl. Acad. Sci. USA 84, 2532–2536.
Beck, A., Jung, G., Gaida, W., Köppen, H., Lang, R., and Schnorrenberg, G. (1989). FEBS Lett. 244, 119–122.
Björnsson, O. G., Adrian, T. E., Dawson, J., McCloy, R. E., Greenburg, G. R., Bloom, S. R., and Chadwick, V. S. (1979). Eur. J. Clin. Invest. 9, 293–301.
Blundell, T. L., Pitts, J. E., Tickle, I. J., Wood, S. P., and Wu, C.-W. (1981). Proc. Natl. Acad. Sci. USA 78, 4175–4179.
Chou, P. Y. and Fasman, G. D. (1978). Annu. Rev. Biochem. 47, 251–276.
Clark, J. T., Kalra, P. S., Crowley, W. R., and Kalra, S. P. (1984). Endocrinology 115, 427–429.
Cosic, I. (1994). IEEE Tran. Biomed. Eng. 41, 1101–1114.
Cosic, I. (1997). In The Resonant Recognition Model of Macromolecular Bioactivity: Theory and Applications, Birkhäuser, Basel.
Cosic, I. and Hearn, M. T. W. (1991). J. Mol. Recognition 4, 57–62.
Cosic, I. and Hearn, M. T. W. (1992). Eur. J. Biochem. 205, 613–619.
Cosic, I. and Nesic, D. (1987). Eur. J. Biochem. 170, 247–252.
Cosic, I., Pavlovic, M., and Vojisavljevic, V. (1989). Biochimie 71, 333–342.
de Vos, A. M., Tong, L., Milburn, M. V., Matias, P. M., Jancarik, J., Noguchi, S., Nishimura, S., Miura, K., Ohtsuka, E., and Kim, S.-H. (1988). Science 239, 888–893.
Emson, P. C. and de Quidt, M. E. (1984). Trends Neurosci. 7, 31–35.
Erickson, J. C., Clegg, K. E., and Palmiter, R. D. (1996). Nature 381, 415–418.
Glover, I., Haneef, I., Pitts, J., Wood, S., Moss, D., Tickle, I., and Blundell, T. (1983). Biopolymers 22, 293–304.
Glover, I. D., Barlow, D. J., Pitts, J. E., Wood, S. P., Tickle, I. J., Blundell, T. L., Tatemoto, K., Kimmel, J. R., Wollmer, A., Strassburger, W., and Zhang, Y.-S. (1985). Eur. J. Biochem. 142, 379–385.
Hoyle, C. H. V. (1996). In Neuropeptides: Essential Data, Wiley, Chichester, U.K.
Krstenansky, J. L., Owen, T. J., Buck, S. H., Hagaman, K. A., and McLean, L. R. (1989). Proc. Natl. Acad. Sci. USA 86, 4377–4381.
Laviano, A., Fanelli, F. R., and Meguid, M. M. (1998). Science 280, 503.
Levine, A. S. and Morley, J. E. (1984). Peptides 5, 1025–1029.
Lundberg, J. M. and Tatemoto, K. (1982). Acta Physiol. Scand. 116, 393–402.
Minakata, H., Taylor, J. W., Walker, M. W., Miller, R. J., and Kaiser, E. T. (1989). J. Biol. Chem. 264, 7907–7913.
Murakami, M. (1985). J. Theor. Biol. 114, 193–198.
Murakami, M. (1987). J. Theor. Biol. 128, 339–347.
Stanley, B. G. and Leibowitz, S. F. (1984). Life Sci. 35, 2635–2642.
Taylor, I. L., Solomon, T. E., Walsh, J. H., and Grossman, M. I. (1979). Gastroenterology 76, 524–528.
Tong, L., de Vos, A. M., Milburn, M. V., Jancarik, J., Noguchi, S., Nishimura, S., Miura, K., Ohtsuka, E., and Kim, S.-H. (1989). Nature 337, 90–93.
Veljkovic, V. and Cosic, I. (1987). Cancer Biochem. Biophys. 9, 139–148.
Veljkovic, V., Cosic, I., Dimitrijevic, B., and Lalovic, D. (1985). IEEE Trans. Biomed. Eng. BME-32, 337–341.
Wolfram, S. (1996). In The Mathematica Book (3rd ed.), Wolfram Media, Champaign, Illinois, pp. 868–869.
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Murakami, M. Resonant Recognition Model of Neuropeptide Y Family: Hot Spot Amino Acid Distribution in the Sequences. J Protein Chem 19, 609–613 (2000). https://doi.org/10.1023/A:1007143113887
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DOI: https://doi.org/10.1023/A:1007143113887