Z1-4071 — Final report
1.
Cys-Ph-TAHA

We synthesized a new lanthanide single thiol reacting tag for the paramagnetic labelling of proteins, named CysPhTAHA, which gives NMR spectra with a single set of peaks. Bound to ubiquitin, it induced large residual dipolar couplings and pseudocontact shifts that could be measured easily and agreed very well with the protein structure. We show that CysPhTAHA can be used to label large proteins that are biochemically challenging such as the Lac repressor in a 90 kDa ternary complex with DNA and inducer.

COBISS.SI-ID: 25010983
2.
Study of complexes between a snake venom or human secreted phospholipase A2 and calmodulin by high-resolution NMR.

In this invited lecture our recent results of the nature of sPLA2-CaM interaction, were presented.

COBISS.SI-ID: 26807847
3.
Study of complexes between a snake venom or human secreted phospholipase A2 and calmodulin by high-resolution NMR.

On the poster our most recent results of the nature of sPLA2-CaM interaction and the inhibitor that prevents the interaction, were presented.

COBISS.SI-ID: 36989189
4.
NMR study of the complex formation between secreted phospholipases A2 and calmodulin.

On the poster our first NMR results of the nature of sPLA2-CaM interaction, were presented.

COBISS.SI-ID: 26286375
5.
Structural insight into LexARecA interaction

Bacterial SOS response play crucial rule in the development of bacterial antibiotic resistance, where a key regulator is a complex formed between single stranded DNA (ssDNA) and two proteins, RecA and LexA. Based on the experimental data we constructed three-dimensional model of a ssDNA-RecA-LexA complex, which offers new possibilities to fight antibiotic resistance of bacteria.

COBISS.SI-ID: 26953767