MSCE  Vol.3 No.12 , December 2015
Computer Simulation Study of Biopolymer Betanova

Betanova is a monomeric, three-stranded antiparallel beta-sheet protein with twenty residues. The pathways between the folded native structure and unfolded conformations of betanova are studied using UNRES force field and the most popular computer simulation method, Metropolis Monte Carlo algorithm. At a fixed temperature, 100 Monte Carlo simulations are performed, starting from the folded native structure, and the pathways are obtained at two different temperatures.

Cite this paper: Kim, S. (2015) Computer Simulation Study of Biopolymer Betanova. Journal of Materials Science and Chemical Engineering, 3, 8-11. doi: 10.4236/msce.2015.312002.

[1]   Creighton, W.E. (1993) Proteins: Structures and Molecular Properties. 2nd Edition, W.H. Freeman and Company, New York.

[2]   Kortemme, T., Ramirez-Alvarado, M. and Serrano, L. (1998) Design of a 20-Amino Acid, Three-Stranded Beta-Sheet Protein. Science, 281, 253-256.

[3]   Lee, J., Kim, S.-Y. and Lee, J. (2004) Design of a Protein Potential Energy Landscape by Parameter Optimization. Journal of Physical Chemistry B, 108, 4525-4534.

[4]   Fishman, G.S. (1996) Monte Carlo: Concepts, Algorithms, and Applications. Springer-Verlag, New York.

[5]   Kim, S.-Y., Lee, J. and Lee, J. (2004) Folding of Small Proteins Using a Single Continuous Potential. Journal of Chemical Physics, 120, 8271-8276.