@article{MTMT:1452809,
	title = {15N and 13C Group‐Selective Techniques Extend the Scope of STD NMR Detection of Weak Host–Guest Interactions and Ligand Screening},
	url = {https://m2.mtmt.hu/api/publication/1452809},
	author = {E Kövér, Katalin and Wéber, Edit and Martinek, Tamás and Monostori, Éva and Batta, Gyula},
	doi = {10.1002/cbic.201000317},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {11},
	unique-id = {1452809},
	issn = {1439-4227},
	abstract = {Saturation transfer difference (STD) is a valuable tool for studying the binding of small molecules to large biomolecules and for obtaining detailed information on the binding epitopes. Here, we demonstrate that the proposed N-15/C-13 variants of group-selective, "GS-STD" experiments provide a powerful approach to mapping the binding epitope of a ligand even in the absence of efficient spin diffusion within the target protein. Therefore, these experimental variants broaden the scope of STD studies to smaller and/or more-dynamic targets. The STD spectra obtained in four different experimental setups (selective H-1 STD, N-15 GS-STD, C-13(Ar) and C-13(aliphatic) GS-STD approaches) revealed that the signal-intensity pattern of the difference spectra is affected by both the type and the spatial distribution of the excited "transmitter" atoms, as well as by the efficiency of the spin-diffusion-mediated magnetization transfer. The performance of the experiments is demonstrated on a system by using the lectin, galectin-1 and its carbohydrate ligand, lactose.},
	keywords = {BINDING; RECEPTOR; PROTEIN; CANCER; SPECTROSCOPY; MOLECULAR RECOGNITION; EXCITATION; lectin; Galectin-1; NMR spectroscopy; molecular dynamics; TRANSFER DIFFERENCE NMR; saturation transfer difference spectroscopy; host-guest chemistry},
	year = {2010},
	eissn = {1439-7633},
	pages = {2182-2187},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Martinek, Tamás/0000-0003-3168-8066; Monostori, Éva/0000-0002-7442-3562; Batta, Gyula/0000-0002-0442-1828}
}