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
, 8-11. doi: 10.4236/msce.2015.312002
 Creighton, W.E. (1993) Proteins: Structures and Molecular Properties. 2nd Edition, W.H. Freeman and Company, New York.
 Kortemme, T., Ramirez-Alvarado, M. and Serrano, L. (1998) Design of a 20-Amino Acid, Three-Stranded Beta-Sheet Protein. Science, 281, 253-256. http://dx.doi.org/10.1126/science.281.5374.253
 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. http://dx.doi.org/10.1021/jp037076c
 Fishman, G.S. (1996) Monte Carlo: Concepts, Algorithms, and Applications. Springer-Verlag, New York.
 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. http://dx.doi.org/10.1063/1.1689643