scholarly journals Helical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles

2016 ◽  
Vol 138 (37) ◽  
pp. 12029-12032 ◽  
Author(s):  
Marvin J. Bayro ◽  
Barbie K. Ganser-Pornillos ◽  
Kaneil K. Zadrozny ◽  
Mark Yeager ◽  
Robert Tycko
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Helical Conformation ◽  
Virus Like Particles ◽  
Hiv 1

scholarly journals Solid-State NMR Studies of HIV-1 Capsid Protein Assemblies

2010 ◽  
Vol 132 (6) ◽  
pp. 1976-1987 ◽  
Author(s):  
Yun Han ◽  
Jinwoo Ahn ◽  
Jason Concel ◽  
In-Ja L. Byeon ◽  
Angela M. Gronenborn ◽  
...  
Keyword(s):  
Solid State ◽  
Capsid Protein ◽  
Solid State Nmr ◽  
Protein Assemblies ◽  
Nmr Studies ◽  
Hiv 1

scholarly journals 1G1115 Interaction of HIV-1 Tat (48-60) peptide with phospholipid membrane by solid state NMR

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S37
Author(s):  
H. Izumi ◽  
S. Toraya ◽  
K. Nishimura ◽  
A. Naito
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Phospholipid Membrane ◽  
Hiv 1

scholarly journals Structure and Orientation of Pardaxin Determined by NMR Experiments in Model Membranes

2004 ◽  
Vol 279 (44) ◽  
pp. 45815-45823 ◽  
Author(s):  
Fernando Porcelli ◽  
Bethany Buck ◽  
Dong-Kuk Lee ◽  
Kevin J. Hallock ◽  
Ayyalusamy Ramamoorthy ◽  
...  
Keyword(s):  
Solid State ◽  
Lipid Bilayers ◽  
Lipid Membranes ◽  
Solid State Nmr ◽  
Double Resonance ◽  
Slow Motion ◽  
Solution Nmr ◽  
Helical Conformation ◽  
Hydrophobic Core ◽  
Nmr Studies

Pardaxins are a class of ichthyotoxic peptides isolated from fish mucous glands. Pardaxins physically interact with cell membranes by forming pores or voltage-gated ion channels that disrupt cellular functions. Here we report the high-resolution structure of synthetic pardaxin Pa4 in sodium dodecylphosphocholine micelles, as determined by1H solution NMR spectroscopy. The peptide adopts a bend-helix-bend-helix motif with an angle between the two structure helices of 122 ± 9°, making this structure substantially different from the one previously determined in organic solvents. In addition, paramagnetic solution NMR experiments on Pa4 in micelles reveal that except for the C terminus, the peptide is not solvent-exposed. These results are complemented by solid-state NMR experiments on Pa4 in lipid bilayers. In particular,13C-15N rotational echo double-resonance experiments in multilamellar vesicles support the helical conformation of the C-terminal segment, whereas2H NMR experiments show that the peptide induces considerable disorder in both the head-groups and the hydrophobic core of the bilayers. These solid-state NMR studies indicate that the C-terminal helix has a transmembrane orientation in DMPC bilayers, whereas in POPC bilayers, this domain is heterogeneously oriented on the lipid surface and undergoes slow motion on the NMR time scale. These new data help explain how the non-covalent interactions of Pa4 with lipid membranes induce a stable secondary structure and provide an atomic view of the membrane insertion process of Pa4.

Structural modeling of Vpu from HIV-1 based on solid-state NMR observables

2014 ◽  
Vol 599 ◽  
pp. 116-121 ◽  
Author(s):  
SeonJoo Ahn ◽  
GyuTae Lim ◽  
Seungyoon Nam ◽  
Jinhyuk Lee
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Structural Modeling ◽  
Hiv 1

Solid state NMR measurements of conformation and conformational distributions in the membrane-bound HIV-1 fusion peptide

2001 ◽  
Vol 19 (1) ◽  
pp. 129-135 ◽  
Author(s):  
Jun Yang ◽  
Paul D Parkanzky ◽  
Bhagyashree A Khunte ◽  
Christian G Canlas ◽  
Rong Yang ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Fusion Peptide ◽  
Membrane Bound ◽  
Hiv 1
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