Abstract
The separation of double-stranded peptide chains can occur in two ways: cooperatively or non-cooperatively. These two regimes can be driven either by chemical or thermal effects, or through non-local mechanical interactions. Here, we show explicitly that local mechanical interactions in biological systems may regulate the stability, the reversibility, and the cooperative/non-cooperative character of the debonding transition. We show that this transition is characterized by a single parameter depending on an internal length scale. Our theory describes a wide range of melting transitions found in biological systems such as protein secondary structures, microtubules and tau proteins, and DNA molecules. In these cases, the theory gives the critical force as a function of the chain length and its elastic properties. Our theoretical results provide quantitative predictions for known experimental effects that appear in different biological and biomedical fields.