Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptide
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Title
Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptide
Authors
Keywords
-
Journal
Scientific Reports
Volume 6, Issue 1, Pages -
Publisher
Springer Nature
Online
2016-06-16
DOI
10.1038/srep28099
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Related references
Note: Only part of the references are listed.- Mechanics of membrane fusion/pore formation
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- The influenza fusion peptide promotes lipid polar head intrusion through hydrogen bonding with phosphates and N-terminal membrane insertion depth
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- Definition and testing of the GROMOS force-field versions 54A7 and 54B7
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- The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface
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- Composition and Functions of the Influenza Fusion Peptide
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- Atomic-Resolution Simulations Predict a Transition State for Vesicle Fusion Defined by Contact of a Few Lipid Tails
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