Stability of SIV gp32 fusion-peptide single-layer protofibrils as monitored by molecular-dynamics simulations

Patricia Soto; Josep Cladera; Alan E. Mark; Xavier Daura

doi:10.1002/anie.200461935

Stability of SIV gp32 fusion-peptide single-layer protofibrils as monitored by molecular-dynamics simulations

Patricia Soto, Josep Cladera, Alan E. Mark, Xavier Daura

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

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	https://doi.org/10.1002/anie.200461935
State	Published - Feb 4 2005
Externally published	Yes

All Science Journal Classification (ASJC) codes

Catalysis
Chemistry(all)

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10.1002/anie.200461935

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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.",

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