NMR Solution Structure of the Trp-Rich Peptide of HIV gp41 Bound to DPC Micelles
The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles.
Minimized Average Structure for this deposition
This peptide was chemically synthesized. The sequence of the peptide is naturally found in Human Immunodeficiency Virus (HIV).
This structure was determined using standard 2D homonuclear techniques.
Structures were initially generated using CNS. Ambiguous and unassigned noe constraints were then used in conjuction with matrix relaxation analysis using the program ARIA.
distance geometry, simulated annealing, molecular dynamics, matrix relaxation
1.6 mM synthetic gp41 peptide, 200 mM perdeuterated dodecylphosphocholine
F.Delaglio, S.Grzesiek, G.Vuister, G.Zhu, J.Pfeifer, A.Bax
A.T.Brunger, P.D.Adams, G.M.Clore, W.L.Delano, P.Gros, R.W.Grosse-Kunstleve, J.-S.Jiang, J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson, G.L.Warren