201. Stability of SIV gp32 Fusion‐Peptide Single‐Layer Protofibrils as Monitored by Molecular‐Dynamics Simulations
- Author
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Patricia Soto, Alan E. Mark, Josep Cladera, Xavier Daura, and Molecular Dynamics
- Subjects
Models, Molecular ,Amyloid ,ANTIPARALLEL ,Protein Conformation ,Recombinant Fusion Proteins ,Molecular Sequence Data ,Retroviridae Proteins, Oncogenic ,Peptide ,protein models ,Curvature ,Catalysis ,Force field (chemistry) ,INFRARED-SPECTROSCOPY ,Molecular dynamics ,DOMAIN ,Viral entry ,Animals ,Humans ,Computer Simulation ,Amino Acid Sequence ,SHEET STRUCTURE ,chemistry.chemical_classification ,Chemistry ,aggregation ,Gene Products, env ,General Chemistry ,General Medicine ,molecular dynamics ,SIMIAN IMMUNODEFICIENCY VIRUS ,SOLID-STATE NMR ,MODEL ,Crystallography ,Solid-state nuclear magnetic resonance ,BETA-AMYLOID FIBRILS ,Biophysics ,FORCE-FIELD ,PARALLEL ,Cattle ,protofibrils ,Peptides ,Viral Fusion Proteins ,Fusion peptide ,Single layer - 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.
- Published
- 2005
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