| Autor: |
Nishikawa, Naohiro, Sakae, Yoshitake, Gouda, Takuya, Tsujimura, Yuichiro, Okamoto, Yuko |
| Zdroj: |
Biophysical Journal; March 2019, Vol. 116 Issue: 5 p781-790, 10p |
| Abstrakt: |
A peptide β2-m21−31, which is a fragment from residue 21 to residue 31 of β2-microgloblin, is experimentally known to self-assemble and form amyloid fibrils. In order to understand the mechanism of amyloid fibril formations, we applied the replica-exchange molecular dynamics method to the system consisting of three fragments of β2-m21−31. From the analyses on the temperature dependence, we found that there is a clear phase transition temperature in which the peptides aggregate with each other. Moreover, we found by the free energy analyses that there are two major stable states: One of them is like amyloid fibrils and the other is amorphous aggregates. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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