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In chemical reactions, inner barriers, which precede the rate-determining transition state, are kinetically invisible but mechanistically significant. On an example of reduction of macrocyclic disulphides, the authors quantify these inner barriers by studying the reaction rate as a function of applied force.
Replicating the functionality of bioactive proteins using rationally designed small molecule mimics is both economically valuable and synthetically challenging. Here the authors develop a mimic of the inflammatory protein C3a with equal biological potency but enhanced stability and bioavailability.
