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 journalArticleResearchpeer-review

15 Citations (Scopus)

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. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish
Pages (from-to)1065-1067
JournalAngewandte Chemie - International Edition
Volume44
DOIs
Publication statusPublished - 4 Feb 2005

Keywords

  • Aggregation
  • Molecular dynamics
  • Peptides
  • Protein models
  • Protofibrils

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