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 |
|---|---|
| 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 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
Cite this
Stability of SIV gp32 fusion-peptide single-layer protofibrils as monitored by molecular-dynamics simulations. / Soto, Patricia; Cladera, Josep; Mark, Alan E.; Daura, Xavier.
In: Angewandte Chemie - International Edition, Vol. 44, No. 7, 04.02.2005, p. 1065-1067.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Stability of SIV gp32 fusion-peptide single-layer protofibrils as monitored by molecular-dynamics simulations
AU - Soto, Patricia
AU - Cladera, Josep
AU - Mark, Alan E.
AU - Daura, Xavier
PY - 2005/2/4
Y1 - 2005/2/4
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=15444364664&partnerID=8YFLogxK
U2 - 10.1002/anie.200461935
DO - 10.1002/anie.200461935
M3 - Article
C2 - 15630707
AN - SCOPUS:15444364664
VL - 44
SP - 1065
EP - 1067
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
SN - 1433-7851
IS - 7
ER -