Molecules. Golič Grdadolnik, Simona (guest editor 2020, member of the editorial board 2020-). Basel: MDPI, 1996-. ISSN 1420-3049. http://www.mdpi.com/journal/molecules. [COBISS.SI-ID 18462981]
C.03 Guest-associated editor
COBISS.SI-ID: 18462981Invited online lecture at the CMSP Seminar (Atomistic Simulation Webinar Series), International Centre for Theoretical Physics, Trieste, Italy, 10. 3. 2021. [COBISS.SI-ID 62269187]
B.04 Guest lecture
COBISS.SI-ID: 62269187Conversational radio show about scientific achievement.
B.06 Other
COBISS.SI-ID: 6635802The capabilities of ligand-based and protein-based NMR methods for the identification and characterization of ligand-protein interactions were presented using the results of our latest studies of ligand binding to the protein target muramyl ligaze D (MurD). Special attention was given to the unique ability of NMR spectroscopy to provide a combined structure-dynamic insight into ligand-protein binding.
B.04 Guest lecture
COBISS.SI-ID: 6691610To describe the molecular determinants of the ATP binding to rhNGF and define its functional roles, the solution NMR structure of rhNGF in the unbound state was determined. The NOEs obtained from the 3D 15N- and 13C-NOESY-HSQC spectra were used for the 3D structural model construction and validation. The solution structure closely resembles those determined by X-ray crystallography for rhNGF-ligand complexes especially as to the topology of the Cys-knot, whereas it exhibits notable differences within the flexible loop regions. Furthermore, in the present NMR structure of unbound rhNGF, the N-terminus is flexible and lacks a specific secondary structure propensity, whereas in the X-ray crystal structures of the rhNGF-TrkA complex, it is involved in the interacting surface and adopts a helicoidal conformation. It is to be noted that this NMR structure represents not only the first solution structure of rhNGF, but the first structure ever for unbound rhNGF.
B.06 Other
COBISS.SI-ID: 14902275