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We show that the interplay between excluded volume effects, hydrophobicity,and hydrogen bonding of a tube-like representation of a polypeptide chain givesrise to free energy landscapes that exhibit a small number of metastable minimacorresponding to common structural motifs observed in proteins. The complexityof the landscape increases only moderately with the length of the chain.Analysis of the temperature dependence of these landscapes reveals that thestability of specific metastable states is maximal at a temperature close tothe mid-point of folding. These mestastable states are therefore likely to beof particular significance in determining the generic tendency of proteins toaggregate into potentially pathogenic agents.

Importance of Metastable States in the Free Energy Landscapes of Polypeptide Chains