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QM and QM/MM modelling of cation-pi interactions – running

Cation-pi interactions play an important role in the chemistry and biology of proteins. The influence the tertiary structure of proteins, and in many cases play a role in ligand recognition and ligand binding to the active site. In the group of Prof. Beáta Vértessy the cytidylyl-choline transferase (CCT) enzyme is experimentally studied, which is one of the key enzyme of the pathogen of malaria. Our work has a two-fold aim. On the one hand we would like to investigate the cation-pi interaction formed between CCT enzyme and its substrate/product, and to examine the role of each amino acid in order to be able to interpret the experimetal results on the thermodynamic parameters of the wild type and mutant enzymes. On the other hand we would like to quantitatively assess the strengths of the cation-pi interaction between choline/phosphocholin and aromatic amino acids. Finally we would like to set up a general model that could be used to predict the binding affinity of choline/phosphocholine to various aromatic sites. We plan to use quantum chemical and combined quantum mechanics molecular mechanics methods.

Project owner:
Dr. Oláh Julianna (Szervetlen és Analitikai Kémia Tanszék)
Members:
Szervetlen és Analitikai Kémia Tanszék (VBK-IAACHEM)
Cooperations:

Természettudományi Kutatóközpont
VBK-ABET