Tertiary structure, mimetics

The basic question of mimetic catalysis is the determination of physicochemical properties of enzymes to be simulated in the synthesized biomimic in accordance with the reaction modeled. Firstly, let us try to answer one of the key questions that arise in biomimic construction how important is it to reach the enzymatic specificity in the synthesis of their analogs To put it another way, should the dynamic (tertiary) structure of the enzyme responsible for the selectivity control mechanism be simulated by active site protection from competitive admixtures This feature of the enzymes distinguishes them from usual catalysts. 

Complexes that feature a-helices at interfaces were studied because a-helices constitute the largest class of protein secondary structure and mediate many protein interactions [30, 51]. Helices located within the protein core are vital for the overall stability of protein tertiary structure, whereas exposed a-helices on protein surfaces constitute central bioactive regions for the recognition of numerous proteins, DNAs, and RNAs. Importantly, helix mimetics have emerged as a highly effective class of PPI inhibitors [32, 36, 44, 52-55]. 

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