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) |
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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)