@article{MTMT:1155933,
	title = {Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape},
	url = {https://m2.mtmt.hu/api/publication/1155933},
	author = {Hetényi, Anasztázia and Szakonyi, Zsolt and Mándity, István and Szolnoki, Éva Tünde and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1039/b812114a},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	unique-id = {1155933},
	issn = {1359-7345},
	abstract = {The long-range side-chain repulsion between the (1R, 2R, 3R, 5R)-2-
		amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid
		(trans-ABHC) residues stabilize the H12 helix in beta-peptide oligomers.},
	keywords = {SECONDARY STRUCTURE; OLIGOMERS; AMINO-ACID; FORM},
	year = {2009},
	eissn = {1364-548X},
	pages = {177-179},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Szakonyi, Zsolt/0000-0003-2432-8409; Mándity, István/0000-0003-2865-6143; Tóth, Gábor/0000-0002-3604-4385; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}