Chain length scaling of protein folding time: Beta sheet structures

K. Dimitrievski, B. Kasemo, V. P. Zhdanov
2000 Journal of Chemical Physics  
We ¤ present comprehensive 3D lattice Monte Carlo simulations of the folding kinetics of two-turn antiparallel ¥ ¦ sheets. § The model employed takes into account isotropic nonspecific interactions as in previous flexible heteropolymer models and also orientation-dependent monomer-monomer interactions, mimicking the formation of hydrogen bonds and chain rigidity. The chain length is varied © from N 15 to 33. For each chain length, we calculate the fastest folding temperature, T fast , folding
more » ... T fast , folding temperature, T fold , and glass-transition temperature, T g . The time-averaged occupation probabilitÿ of the native state is found to be nearly independent of N at 1 3 2 2.7-4.0 at T 4 T fast and ¥ 5.2 at T slightly § below T fold . Evaluating 5 6 f # in $ real units at T near 7 T fold yields 8 physically reasonable results. © 2000 9 American Institute @ of Physics.
doi:10.1063/1.481915 fatcat:yahl7ym2xncqdkvc4a3rcgszkm