| Hauptseite > Publikationsdatenbank > Early amyloid β-protein aggregation precedes conformational change > print |
| 001 | 150941 | ||
| 005 | 20210129213333.0 | ||
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| 100 | 1 | _ | |a Barz, Bogdan |0 P:(DE-Juel1)151182 |b 0 |u fzj |
| 245 | _ | _ | |a Early amyloid β-protein aggregation precedes conformational change |
| 260 | _ | _ | |a Cambridge |c 2014 |b Soc. |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 520 | _ | _ | |a The aggregation of amyloid-β protein (1–42) is studied at experimental concentrations using all-atom molecular dynamics simulations. We observe a fast aggregation into oligomers without significant changes in the internal structure of individual proteins. The aggregation process is characterized in terms of transition networks. |
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| 700 | 1 | _ | |a Olubiyi, Olujide O. |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Strodel, Birgit |0 P:(DE-Juel1)132024 |b 2 |e Corresponding author |u fzj |
| 773 | _ | _ | |a 10.1039/c3cc48704k |g p. 10.1039.c3cc48704k |0 PERI:(DE-600)1472881-3 |n 40 |p 5373-5375 |t Chemical communications |v 50 |y 2014 |x 1364-548X |
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