Solution NMR structure of gp41 ectodomain monomer on a DPC micelle

gp41 ectodomain monomer on a DPC micelle

Proceedings of the National Academy of Sciences of the United States of America
Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion.

Interactions Between Hiv-1 Gp41 Core And Detergents And Their Implications For Membrane Fusion

Helical Interactions In The Hiv-1 Gp41 Core Reveals Structural Basis For The Inhibitory Activity Of Gp41 Peptides

Crystal Structure Analysis Of The Gp41 Core Mutant

Crystal Structure Analysis Of Gp41 Core Mutant

Inhibition Of Hiv-1 Infectivity By The Gp41 Core: Role Of A Conserved Hydrophobic Cavity In Membrane Fusion

Atomic Structure Of A Thermostable Subdomain Of Hiv-1 Gp41

Crystal Structure Of The Hiv Gp41 Core With The Enfuvirtide Resistance Mutation N43d

Structure Of A Longer Thermalstable Core Domain Of Hiv-1 Gp41 Containing The Enfuvirtide Resistance Mutation N43d

triple labelled (2H/15N/13C) CoreS sample (gp41 ectodomain construct:S546-R579-SGGRG-W628-K655) in solution containing 100 mM DPC

triple labelled (2H/15/13C) CoreS sample in 5.5% acrylamide gel containing 30% cationic DADMAC-acrylamide copolymer. Compressed from 6 mm to 4.1 mm.

Schwieters, Kuszewski, Tjandra and Clore