Nekovalentní interakce aromatických systémů a jejich význam v proteinech a organokatalýze

Biedermannová, Lada

7 Concluding Remarks The aim of the presented thesis was to investigate the interactions of aromatic groups and their role in the processes of chemical and biological recognition. In particular, the role of aromatic residues in the protein hydrophobic core for the stability of the protein native fold was investigated using highJevel quantum chemical calculations. We showed that the interactions of aromatic residues not only with other aromatic and aliphatic sidechains but also with the peptide bond portion of the protein backbone can provide a substantial contribution to the protein stabilisation. Two more specific examples ofthe aromatic interactions, the interaction ofaromatic residue with proline and the aromatic-peptide bond interaction were both examined in more detail. The chapter on the IEM focused on aromatic interactions from the perspective ofall the pairwise residue interactions in protein. The aromatic residues were shown to play a key rolě in the stabilisation of the Trp-cage model protein. It was also shown that the IEM can be used as a reliable method for the identification ofthese key residues. Several computational methods were tested and it was shown that when used with the Amber parm94 foréefie|d and GB solvent model, the IEM gives satisfactory results while being computationally feasible...

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