Abstract
The tetramerization of melittin, a 26-amino-acid peptide, is considered as a model for protein folding. The Monte Carlo simulation was used to study the folding arrangement of melittin, and the results are compared with the experiment. An acceptance rate of 50% for new configurations is achieved by using ranges of ±0.001 Å for the translations and ±15°C for the rotations. Around 311 K, the folded structure of the protein has the greatest stability; the range from −40 to −80 shows the best ϕ angles for melittin. The final optimized structure of melittin strongly depends on the temperature. The melittin tetramer is found to have a temperature of maximum stability ranging from 35.5 to 43°C.
Similar content being viewed by others
References
S. C. Quay and C. C. Condie, Biochemistry 22, 659 (1983).
T. C. Terwillinger and D. Eisenberg, J. Biol. Chem. 257, 6010 (1982).
T. C. Terwillinger and D. Eisenberg, J. Biol. Chem. 257, 6016 (1982).
F. Inagaki, I. Shimada, K. Kawaguchi, et al., Biochemistry 28, 5985 (1989).
R. Bazzo, M. J. Tappin, A. Pastore, et al., Eur. J. Biochem. 173, 139 (1988).
M. Iwadate, T. Asakura, and M. P. Williamson, Eur. J. Biochem. 257, 479 (1998).
K. Ramalingam, S. Aimoto, and J. Bello, Biopolymers 32, 981 (1992).
M. van Veen, G. N. Georgiou, A. F. Drake, and R. J. Cherry, Biochem. J. 305, 7857 (1995).
Y. Sakakibara, M. Brown, R. Hughey, et al., Nucleic Acids Res. 22, 5112 (1994).
E. Habermann and J. Jentsch, Physiol. Chem. 348, 37 (1967).
W. Wilcox and D. Eisenberg, Protein Sci. 1, 641 (1992).
A. P. Demchenko, A. S. Ladokhin, E. G. Kostrzhewskaya, and T. L. Dibrova, Mol. Biol. 21, 663 (1987).
J. F. Faucon, J. Dufourcq, and C. Lussan, FEBS Lett. 102, 187 (1979).
M. Smoluch, M. Gorseling, C. Gooijer, and G. Zwan, J. Fluoresc. 14(1), 37 (2004).
K. A. Dill, Biochemistry 29, 71337 (1990).
T. E. Creighton, Protein Folding (W. H. Freeman, New York, 1992), pp. 1–547.
J.-L. Popot, Curr. Opin. Struct. Biol. 3, 532 (1993).
S.H. White, W.C. Wimley, Curr. Opin. Struct. Biol. 4, 79 (1994).
Membrane Protein Structure: Experimental Approaches, Ed. by S. H. White (Oxford Univ., Oxford, 1994), pp. 1–359.
D. C. Rees, A. J. Chirino, K.-H. Kim, and H. Komiya, in Membrane Protein Structure: Experimental Approaches, Ed. by S. H. White (Oxford Univ., Oxford, 1994), pp. 3–26.
F. M. Richards, in Protein Folding, Ed. by: T. E. Creighton (W. H. Freeman, New York, 1992), pp. 1–58.
P.L. Privalov, in Protein Folding, Ed. by: T.E. Creighton (W. H. Freeman, New York, 1992), pp. 83–126.
C. N. Pace, Methods Enzymol. 131, 266 (1986).
T. Haltia and E. Freire, Biochim. Biophys. Acta 1241, 295 (1995).
K. Ramalingam, J. Bello, and S. Aimoto, FEBS Lett. 295, 200 (1991).
K. Niefind and D. Schomburg, J. Mol. Biol. 219, 481 (1991).
Y. Sugita, A. Kitao, and Y. Okamoto, J. Chem. Phys. 113, 6042 (2000).
E. Lyman, F. M. Ytreberg, and D. M. Zuckerman, Phys. Rev. Lett. (in press).
N. Rathore and J. de Pablo, J. Chem. Phys. 116, 7225 (2002).
B. R. Brooks, R. E. Bruccoleri, B. D. Olafson, et al., J. Comput. Chem. 4, 187 (1983).
N. Metropolis, A. W. Rosenbulth, M. N. Rosenbulth, et al., J. Chem. Phys. 21, 1087 (1953).
P. J. Steinbach, Proteins, p. 6656 (2004).
Author information
Authors and Affiliations
Additional information
The text was submitted by the authors in English.
Rights and permissions
About this article
Cite this article
Monajjemi, M., Ketabi, S. & Amiri, A. Monte Carlo simulation study of melittin: Protein folding and temperature dependence. Russ. J. Phys. Chem. 80 (Suppl 1), S55–S62 (2006). https://doi.org/10.1134/S0036024406130103
Received:
Issue Date:
DOI: https://doi.org/10.1134/S0036024406130103