@article{MTMT:2347492,
	title = {Foldameric β-H18/20P mixed helix stabilized by head-to-tail contacts: A way to higher-order structures Foldameric-H18/20P Mixed Helix Stabilized by Head-to-Tail Contacts: A Way to Higher-Order Structures},
	url = {https://m2.mtmt.hu/api/publication/2347492},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Mándity, István and Fülöp, Ferenc and Martinek, Tamás},
	doi = {10.1002/ejoc.201201633},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2013},
	unique-id = {2347492},
	issn = {1434-193X},
	abstract = {Peptidic foldamers are known to exhibit increased diversity in the periodic secondary-structure space in comparison with their natural counterparts, but their higher-order self-organization has been studied less thoroughly. In theory, large-diameter peptide foldamer helices have the capability of self-recognition through axial helix-helix interactions (e.g., head-to-tail), but this phenomenon has previously been observed in only one instance. In this article we report on the discovery of the largest-diameter β-peptidic mixed helix to date, the H18/20P helix. Its formation is solvent-dependent and its folding occurs cooperatively through head-to-tail self-assembly in solution. These findings suggest that axial helix-helix interactions can serve as a new mode for the formation of tertiary/quaternary structures for peptide foldamers, which also show higher-order structural diversity than natural proteins. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
	keywords = {PEPTIDES; FOLDAMERS; Protein Folding; amino acids; self-assembly; helical structures},
	year = {2013},
	eissn = {1099-0690},
	pages = {3555-3559},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066}
}