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The terms intermolecular and intramolecular recognition are often used when referring to binding and folding, highlighting the common ground between the two processes. Most studies, however, are aimed at either one process or the other. Here, we show how knowledge from binding can aid in understanding folding and vice versa.
Background: It has been observed that single-domain proteins and domains in multidomain proteins favor a chain length in the range 100–50 amino acids. To understand the origin of the favored size, we construct an empirical function for the free energy of unfolding versus the chain length. The parameters in the function are derived by fitting to the energy of hydration, entropy and enthalpy of unfolding...
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