Document Type

Article

Publication Date

11-1-2004

Department

Physics and Astronomy

Abstract

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 R(g) with the molecular weight N R(g) proportional to N(gamma) with gamma similar or equal to 3/5. Specific interactions with longer range and higher strength are needed to approach the native globular conformations with gamma< 3/5. Relaxation into the globular ground state shows a weak power-law decay, i.e., R(g) proportional to t(-alpha), alpha similar to 0.06-0.12.

Comments

©Physical Review E

Publisher Version

Publication Title

Physical Review E

Volume

70

Issue

5

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