Abstract
Molecular recognition is at the core of the design of any supramolecular system. Proteins, because of their biological relevance and structural complexity, provide us with exquisite examples of molecular recognition in a natural setting. Most of the effort reported in the literature towards the design of artificial compounds able to bind proteins with high affinity and selectivity has been targeted to rather hydrophobic areas: the design of enzyme inhibitors could be the paradigm of such studies, the inhibitor being designed to occupy a groove on the protein surface where the active center of the enzyme is located [1].
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Salvatella, X. et al. (1999). Protein Surface Recognition. In: Pons, M. (eds) NMR in Supramolecular Chemistry. NATO ASI Series, vol 526. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4615-9_17
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DOI: https://doi.org/10.1007/978-94-011-4615-9_17
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