TY  - JOUR
AU  - Németh, Lukács
AU  - Hegedüs, Zsófia
AU  - Martinek, Tamás
TI  - Predicting Order and Disorder for β-Peptide Foldamers in Water
JF  - JOURNAL OF CHEMICAL INFORMATION AND MODELING
J2  - J CHEM INF MODEL
VL  - 54
PY  - 2014
IS  - 10
SP  - 2776
EP  - 2783
PG  - 8
SN  - 1549-9596
DO  - 10.1021/ci5003476
UR  - https://m2.mtmt.hu/api/publication/2764648
ID  - 2764648
AB  - 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.
LA  - English
DB  - MTMT
ER  -