Abstract
Modeling the mechanisms of protofibril twisting: Molecular-dynamics simulations of simian viral peptide aggregates show that β sheets of 10 to 30 chains form left-handed helical ribbons with saddlelike curvature (see picture). These structures are highly dynamic, with oscillations around an average twist angle of 9-10°, and a pitch of 15-20 nm, depending on β-sheet length. The peptides studied are key to viral entry into host cells.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1065-1067 |
| Number of pages | 3 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 44 |
| Issue number | 7 |
| DOIs | |
| State | Published - Feb 4 2005 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
Fingerprint Dive into the research topics of 'Stability of SIV gp32 fusion-peptide single-layer protofibrils as monitored by molecular-dynamics simulations'. Together they form a unique fingerprint.
Cite this
Soto, P., Cladera, J., Mark, A. E., & Daura, X. (2005). Stability of SIV gp32 fusion-peptide single-layer protofibrils as monitored by molecular-dynamics simulations. Angewandte Chemie - International Edition, 44(7), 1065-1067. https://doi.org/10.1002/anie.200461935