scholarly journals Quantifying the fraction of alanine residues in an α-helical conformation in hornet silk using solid-state NMR

2012 ◽  
Vol 44 (8) ◽  
pp. 876-881 ◽  
Author(s):  
Tsunenori Kameda
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Helical Conformation

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 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.

A useful tool for the elaboration of new solid-state NMR experiments: PULSAR

1995 ◽  
Vol 92 ◽  
pp. 1939-1942 ◽  
Author(s):  
JP Amoureux ◽  
C Fernandez ◽  
Y Dumazy
Keyword(s):  
Solid State ◽  
Solid State Nmr

Quantitative analysis by 13C solid-state NMR of eumelanins

1994 ◽  
Vol 91 ◽  
pp. 881-887 ◽  
Author(s):  
M Hervé ◽  
J Hirschinger ◽  
P Granger ◽  
P Gilard ◽  
N Goetz
Keyword(s):  
Quantitative Analysis ◽  
Solid State ◽  
Solid State Nmr

Structural Analysis of Slag and Cement Materials by Solid-state NMR

2018 ◽  
Vol 56 (5) ◽  
pp. 454-459
Author(s):  
T. Takahashi ◽  
T. Ohkubo ◽  
K. Kanehashi
Keyword(s):  
Solid State ◽  
Structural Analysis ◽  
Solid State Nmr
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