In biology, there are several processes in which unfolded protein chains are transported along narrow tube channels. Normally, without such a severe configurational constraint, unfolded polypeptides would not bind to each other. However, when chain entropy is much reduced in the narrow channel, we find that polypeptide chains prefer to bind, even if there is no great potential energy gain in doing so. We find the expressions for average length of binding  (the number of monomers at the chain ends that form bonds) and the critical tube diameter at which such constrained binding occurs  .
In biology, there are several processes in which unfolded protein chains are transported along narrow-tube channels. Normally, without such a severe configurational constraint, unfolded polypeptides would not bind to each other. However, when chain entropy is much reduced in the narrow channel, we find that polypeptide chains have a propensity to bind, even if there is no great potential energy gain in doing so. We find the average length of binding m* (the number of monomers at the chain ends that form bonds) and the critical tube diameter at which such constrained binding occurs . We carry out Brownian dynamics simulations of tightly confined chains, demonstrating their binding over the characteristic length m*, changing in tubes of different diameter .
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. We carry out Brownian dynamics simulations of tightly confined chains, demonstrating their binding over the characteristic length m*, changing in tubes of different diameter