@article{MTMT:3148106,
	title = {Target-specific NMR detection of protein–ligand interactions with antibody-relayed 15N-group selective STD},
	url = {https://m2.mtmt.hu/api/publication/3148106},
	author = {Hetényi, Anasztázia and Hegedüs, Zsófia and Fajka-Boja, Roberta and Monostori, Éva and E Kövér, Katalin and Martinek, Tamás},
	doi = {10.1007/s10858-016-0076-3},
	journal-iso = {J BIOMOL NMR},
	journal = {JOURNAL OF BIOMOLECULAR NMR},
	volume = {66},
	unique-id = {3148106},
	issn = {0925-2738},
	abstract = {Fragment-based drug design has been successfully applied to challenging targets where the detection of the weak protein-ligand interactions is a key element. H-1 saturation transfer difference (STD) NMR spectroscopy is a powerful technique for this work but it requires pure homogeneous proteins as targets. Monoclonal antibody (mAb)-relayed N-15-GS STD spectroscopy has been developed to resolve the problem of protein mixtures and impure proteins. A N-15-labelled target-specific mAb is selectively irradiated and the saturation is relayed through the target to the ligand. Tests on the anti-Gal-1 mAb/Gal-1/lactose system showed that the approach is experimentally feasible in a reasonable time frame. This method allows detection and identification of binding molecules directly from a protein mixture in a multicomponent system.},
	keywords = {BINDING; MEMBRANE-PROTEINS; ANTIBODY; SPECTROSCOPY; DRUG DISCOVERY; TRANSFER DIFFERENCE NMR; Protein-ligand interaction; Biochemistry & Molecular Biology; GS-STD; Protein mixture},
	year = {2016},
	eissn = {1573-5001},
	pages = {227-232},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Hegedüs, Zsófia/0000-0002-5546-8167; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}