@article{MTMT:2764648,
	title = {Predicting Order and Disorder for β-Peptide Foldamers in Water},
	url = {https://m2.mtmt.hu/api/publication/2764648},
	author = {Németh, Lukács and Hegedüs, Zsófia and Martinek, Tamás},
	doi = {10.1021/ci5003476},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {54},
	unique-id = {2764648},
	issn = {1549-9596},
	abstract = {Following a quantitative validation approach, we tested the AMBER ff03 and GAFF force fields with the TIP3P explicit water model in molecular dynamic simulations of beta-peptide foldamers. The test sequences were selected to represent a wide range of folding behavior in water: compact helix, strand mimetic geometry, and the state of disorder. The combination AMBER ff03-TIP3P successfully predicted the experimentally observed conformational properties and reproduced the NOE distances and backbone (3)J coupling data at a good level. GAFF was unable to produce folded structures correctly due to its biased torsion potentials. We can recommend AMBER ff03-TIP3P for simulations involving beta-peptide sequences in aqueous media including ordered and disordered structures.},
	year = {2014},
	eissn = {1549-960X},
	pages = {2776-2783},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Martinek, Tamás/0000-0003-3168-8066}
}