Physics and Astronomy
Mathematics and Natural Sciences
The conformation and dynamics of a protein chain with hydrophobic and polar nodes are examined by the bond-fluctuation model using Monte Carlo simulations on a cubic lattice. The minimal (nearest neighbor) interaction leads to standard (self-avoiding walk) conformation, i.e., the scaling of the radius of gyration Rg with the molecular weight N Rg ∝ Nγ with γ ≃ 3/5/ Specific interactions with longer range and higher strength are needed to approach the native globular conformations with γ < 3/5. Relaxation into the globular ground state shows a weak power-law decay, i.e., Rg ∝ t-α, α ~ 0.06-0.12.
Physical Review E
Pandey, R. B.
(2004). Relaxation to Native Conformation of a Bond-Fluctuating Protein Chain With Hydrophobic and Polar Nodes. Physical Review E, 70(5).
Available at: https://aquila.usm.edu/fac_pubs/2988