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 › Research › peer-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 language	English
Pages (from-to)	1065-1067
Journal	Angewandte Chemie - International Edition
Volume	44
DOIs	https://doi.org/10.1002/anie.200461935
Publication status	Published - 3 Jan 2005

Keywords

Aggregation
Molecular dynamics
Peptides
Protein models
Protofibrils

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10.1002/anie.200461935

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

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. {\textcopyright} 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.",

keywords = "Aggregation, Molecular dynamics, Peptides, Protein models, Protofibrils",

author = "Patricia Soto and Josep Cladera and Mark, {Alan E.} and Xavier Daura",

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doi = "10.1002/anie.200461935",

language = "English",

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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 - 2005/1/3

Y1 - 2005/1/3

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. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

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. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

KW - Aggregation

KW - Molecular dynamics

KW - Peptides

KW - Protein models

KW - Protofibrils

U2 - 10.1002/anie.200461935

DO - 10.1002/anie.200461935

M3 - Article

SN - 1433-7851

VL - 44

SP - 1065

EP - 1067

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

ER -

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

Abstract

Keywords

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