Using the hepatitis C virus p7 hexamer as a representative of proteins with complex transmembrane topology, this work characterizes early lipid-driven dimerization using molecular dynamics simulations.
First-pass extracted concept
hepatitis C virus p7 hexamer
Candidate: concept label1 source documents4 linked claims
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Aliases
p7 hexamer
Evidence Snippets
Supporting Sources
Linked Claims
Membrane lipids are essential, dynamic contributors to protein binding and aggregation in cellular membranes.
Quoted textsource-backed
This study demonstrates that membrane lipids are essential, dynamic contributors to protein binding and aggregation in cellular membranes.
Compared with aqueous solution, a lipid membrane model reveals that protein-lipid interactions critically guide inter-protein residue alignment and binding during p7 dimer interactions.
Quoted textsource-backed
Comparing dimer interactions in aqueous solution versus on a lipid membrane model reveal that protein-lipid interactions critically guide inter-protein residue alignment and binding.
Hydrophobic contacts and hydrogen bonding between key residues and phosphatidylcholine/phosphatidylinositol lipids drive helix interactions that promote p7 oligomerization, particularly involving the first helix.
Quoted textsource-backed
Hydrophobic contacts and hydrogen bonding between key residues and phosphatidylcholine/phosphatidylinositol lipids drive essential helix interactions that promote p7 oligomerization, particularly involving the first helix.
Molecular dynamics simulations characterize early lipid-driven dimerization of hepatitis C virus p7.
Quoted textsource-backed
Using the hepatitis C virus p7 hexamer as a representative of proteins with complex transmembrane topology, this work characterizes early lipid-driven dimerization using molecular dynamics simulations.