中国物理B ›› 2004, Vol. 13 ›› Issue (9): 1574-1581.doi: 10.1088/1009-1963/13/9/037
• 8000 CROSSDISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY • 上一篇 下一篇
吉高峰, 薛彬, 王炜
Ji Gao-Feng (吉高峰), Xue Bin (薛彬), Wang Wei (王炜)
摘要: Using Monte Carlo simulations, we have studied the folding dynamics and thermodynamics of geometrically constrained lattice protein model chains. The constraints are realized by fixing one or both terminals of the chains. By comparing the results with that of the free-end chains, we find that the folding behaviours of the end-constrained chains are not completely similar to that of the free-end chains. Both kinds of constraints on the chain ends affect the folding dynamics of the chains: i.e., the folding rate, but not the thermodynamics. The thermodynamic behaviour of the one-end-fixed chains shows less difference from that of the free-end chains, while the thermodynamic behaviour of the two-end-fixed chains has obvious difference from that of the free-end chains. The origin of these differences comes from the differences of the ergodicity of the chains in the conformational space.
中图分类号: (Folding: thermodynamics, statistical mechanics, models, and pathways)