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Stability of SIV gp32 Fusion‐Peptide Single‐Layer Protofibrils as Monitored by Molecular‐Dynamics Simulations
Author(s) -
Soto Patricia,
Cladera Josep,
Mark Alan E.,
Daura Xavier
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200461935
Subject(s) - molecular dynamics , peptide , curvature , biophysics , fusion , twist , materials science , dynamics (music) , structural stability , crystallography , chemical physics , chemistry , physics , biology , geometry , biochemistry , computational chemistry , mathematics , linguistics , philosophy , structural engineering , acoustics , engineering
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.