We investigate the time evolution of the heteropolymer model introduced by
Iori, Marinari and Parisi to describe some of the features of protein folding
mechanisms. We study how the (folded) shape of the chain evolves in time. We
find that for short times the mean square distance (squared) between chain
configurations evolves according to a power law, D∼tν. We discuss
the influence of the quenched disorder (represented by the randomness of the
coupling constants in the Lennard-Jones potential) on value of the critical
exponent. We find that ν decreases from 32 to 21 when
the strength of the quenched disorder increases.Comment: 12 pages, very simple LaTeX file, 6 figures not included, sorry. SCCS
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