An approach towards structure elucidation of bilitranslocase, the membrane protein which transports bilirubin from blood to liver cells, is shown. Known 3D structures of the trans-membrane domains (PDBTM) are used to build a model for prediction of trans-membrane segments. We also tested a set of non-congeneric compounds for their competitive inhibition in the investigated biomolecular system. The information about chemical structure of small molecules that either pass or block the transmembrane path helps us to biuld a hypothesis about the transport mechanism of the studied biological system.
B.04 Guest lecture
COBISS.SI-ID: 4559130PhD thesis included the study of inhibition of bilitranslocase, a trans membrane protein, whose primary function is the transfer of bilirubin from blood to liver cells. We have tested the interaction with purine, pyrimidines and their derivatives. Information on chemical structure and inhibition constants were used to construct models with artificial neural networks. Correct classification of compounds and good predictive ability was achieved by counter-propagation neural network model coupled with a genetic algorithm; RMS error for the validation set was 0.47 log units of binding affinity.
D.09 Tutoring for postgraduate students
COBISS.SI-ID: 250510848