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Influence of Medium and Long Range Interactions in Different Structural Classes of Globular Proteins

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Abstract

An analysis of the dependence known three dimensional structure ofglobular proteins on their residue contacts and their interactions providesmuch information about their folding and stability. In this work, we analysethe residue-residue contacts and the role of medium and long rangeinteractions in globular proteins belonging to different structural classes.The results show that while medium range interactions predominate in allalpha class proteins, long range interactions predominate in all beta class.The residues Pro and Gly are found to have lowest medium range contacts,probably due to their helix breaking tendency. The hydrophobic residues Ile,Val and Tyr have higher long range contacts, and hence may serve as goodnucleation centres. Further, the role of charged residues and disulfidebridges in these interactions are also discussed.

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References

  1. Nagano, K. and Ponnuswamy, P.K.: Adv. Biophys. 18(1984), 115–148.

    Google Scholar 

  2. Barlow, D.J. and Thornton, J.M.: Biopolymers 25(1986), 1717–1733.

    Google Scholar 

  3. MacArthur, M.W. and Thornton, J.M.: J. Mol. Biol. 218(1991), 397–412.

    Google Scholar 

  4. Karpeisky, M.Ya and Ilyin, V.A.: J. Mol. Biol. 224(1992), 629–638.

    Google Scholar 

  5. Zhu, B-Y., Zhou, N.E., Kay, C.M. and Hodges, R.S.: Protein Sci. 2(1993), 383–394.

    Google Scholar 

  6. Vtyurin, N.: Proteins 15(1993), 62–70.

    Google Scholar 

  7. Ponnuswamy, P.K. and Gromiha, M.M.: J. Theor. Biol. 166(1994), 63–74.

    Google Scholar 

  8. Gobel, U., Sander, C., Schneider, R. and Valencia, A.: Proteins 18(1994), 309–317.

    Google Scholar 

  9. Tanaka, S. and Scheraga, H.A.: Macromolecules 9(1976), 945–950.

    Google Scholar 

  10. Manavalan, P. and Ponnuswamy, P.K.: Arch. Biochem. Biophys. 184(1977), 476–487.

    Google Scholar 

  11. Warme, P.K. and Morgan, R.S.: J. Mol. Biol. 118(1978), 289–304.

    Google Scholar 

  12. Narayana, S.V.L. and Argos, P.: Int. J. Peptide Protein Res. 24(1984), 25–39.

    Google Scholar 

  13. Viswanathan, V.N.: Int. J. Biol. Macromol. 9(1987), 39–48.

    Google Scholar 

  14. Miyazawa, S. and Jernigan, R.L.: Macromolecules 18(1985), 534–552.

    Google Scholar 

  15. Burlety, S.K. and Petsko, G.A.: Science 229(1985), 23–29.

    Google Scholar 

  16. Burtley, S.K. and Petsko, G.A.: Adv. Protein Chem. 39(1988), 125–189.

    Google Scholar 

  17. Heringa, J. and Argos, P.: J. Mol. Biol. 220(1991), 151–171.

    Google Scholar 

  18. Magalhaes, A., Margret, B., Hoflack, J., Gomes, J.N. and Scheraga, H.A.: J. Protein Chem. 13 (1994), 195–215.

    Google Scholar 

  19. Muthusamy, R. and Ponnuswamy, P.K. J. Theor. Biol. 153(1991), 25–40.

    Google Scholar 

  20. Karlin, S., Zucker, M. and Brocchieri, L.: J. Mol. Biol. 239 (1994), 227–248.

    Google Scholar 

  21. Tanaka, S. and Scheraga, H.A.: Proc. Natl. Acad. Sci. 72(1975), 3802–3806.

    Google Scholar 

  22. Ponnuswamy, P.K., Warme, P.K. and Scheraga, H.A.: Proc. Natl. Acad. Sci. USA 70(1973), 830–833.

    Google Scholar 

  23. Allewell, N.: Trends. Biochem. Sci. 16(1991), 239–240.

    Google Scholar 

  24. Tudos, E., Fiser, A. and Simon, I.: Int. J. Peptide Protein Res. 43(1994), 205–208.

    Google Scholar 

  25. Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer, E.F. Jr, Brice, M.O., Rodgers, J.K., Kennard, O., Shimanouchi, T. and Tasumi, M.: J. Mol. Biol. 112(1977), 535–542.

    Google Scholar 

  26. Manavalan, P. and Ponnuswamy, P.K.: Nature 275(1978), 673–674.

    Google Scholar 

  27. Ponnuswamy, P.K., Prabakaran, M. and Manavalan, P. Biochim. Biophys. Acta 623(1980), 301–316.

    Google Scholar 

  28. Shin, Y.A. and Yoo, S.E.: Biopolymers 38(1996), 183–190.

    Google Scholar 

  29. Fasman, G.D. In Prediction of Protein Structure and Principles of Protein Conformation(G.D. Fasman, ed.), pp. 193–316. New York: Plenum Press, 1989.

    Google Scholar 

  30. Gromiha, M.M. and Ponnuswamy, P.K.: Int. J. Peptide Protein Res. 45(1995), 225–240.

    Google Scholar 

  31. Levin, J.M. and Garnier, J. Biochim. Biophys. Acta 955(1988), 283–295.

    Google Scholar 

  32. Rost, B., Schneider, R. and Sander, C.: Trends. Biochem. Sci. 18(1993), 120–123.

    Google Scholar 

  33. Thornton, J.M.: J. Mol. Biol. 151(1981), 261–287.

    Google Scholar 

  34. Matthews, B.W.: Ann. Rev. Biochem. 62(1993), 139–160.

    Google Scholar 

  35. Barlow, D.J. and Thornton, J.M.: J. Mol. Biol. 168(1983), 867–885.

    Google Scholar 

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Gromiha, M.M., Selvaraj, S. Influence of Medium and Long Range Interactions in Different Structural Classes of Globular Proteins. Journal of Biological Physics 23, 151–162 (1997). https://doi.org/10.1023/A:1004981409616

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  • DOI: https://doi.org/10.1023/A:1004981409616

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