Integration and analysis of the effects of an unnatural amino acid into transmembrane 4 of the Orai1 protein

Bc. et Bc. Helene Sabine GEMEINHARDT

Master's thesis

Intergration and analysis of the effects of an unnatural amino acids into transmembrane 4 or the Orai1 protein

Abstract:

In this work intramolecular interactions of the Orai1 protein are investigated by integrating the unnatural amino acid p-Azido-L-phenylalanine (Azi) at different positions (A254, V252 and G247) of the Orai's transmembrane domain 4 (TM4). The compound Azi is unreactive under physiological conditions but can be activated using UV-light. Being reactive it can form covalent bonds with nearby residues. It is suspected that that residue A254 on TM4 is close enough to TM3 for the Azi to cross-link these two transmembrane domains. Positions V252 and G247 are assumed to be too far apart for crosslinking.

Abstract:

In this work intramolecular interactions of the Orai1 protein are investigated by integrating the unnatural amino acid p-Azido-L-phenylalanine (Azi) at different positions (A254, V252 and G247) of the Orai's transmembrane domain 4 (TM4). The compound Azi is unreactive under physiological conditions but can be activated using UV-light. Being reactive it can form covalent bonds with nearby residues. It is suspected that that residue A254 on TM4 is close enough to TM3 for the Azi to cross-link these two transmembrane domains. Positions V252 and G247 are assumed to be too far apart for crosslinking.

Keywords

Orai1, TM4, intramolecular protein interactions, unnatural amino acid, p-Azido-L-phenylalanine

Jazyk práce: English

Datum vytvoření / odevzdání či podání práce: 12. 12. 2023

Obhajoba závěrečné práce

• Vedúci: Dr. Isabella Derler

UNIVERSITY OF SOUTH BOHEMIA IN ČESKÉ BUDĚJOVICE

Faculty of Science

Master programme / odbor:
Biological Chemistry / Biological Chemistry