Çağdaş Dağ

This study identifies two distinct conformational equilibria in arrestin-2 that underlie its pre-activation state in solution.

This study examines how different M9-based media compositions affect E. coli metabolism during recombinant protein expression, finding that M9++ reduces overflow metabolites and promotes biosynthesis.

This study uses SAXS to show that the HERC5 HECT domain forms a trimer in solution, suggesting trimerization may regulate its function.

This paper presents the NMR structure and functional analysis of the Uba7 UFD domain and its interaction with UbcH8, revealing structural flexibility and key residues critical for E2 recognition in the ISGylation pathway.

This study investigates E. coli metabolism on pyruvate as the sole carbon source for NMR studies, revealing metabolic inefficiencies that impact isotopic labeling.