scholarly journals Alamethicin Supramolecular Organization in Lipid Membranes from 19F Solid-State NMR

2016 ◽  
Vol 111 (11) ◽  
pp. 2450-2459 ◽  
Author(s):  
Evgeniy S. Salnikov ◽  
Jesus Raya ◽  
Marta De Zotti ◽  
Ekaterina Zaitseva ◽  
Cristina Peggion ◽  
...  
Keyword(s):  
Solid State ◽  
Lipid Membranes ◽  
Solid State Nmr ◽  
Supramolecular Organization

Rhodopsin Activation in Lipid Membranes Based on Solid-State NMR Spectroscopy

2019 ◽  
pp. 1-16
Author(s):  
Suchithranga M. D. C. Perera ◽  
Xiaolin Xu ◽  
Trivikram R. Molugu ◽  
Andrey V. Struts ◽  
Michael F. Brown
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Lipid Membranes ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy

Structural and Dynamical Changes of the Bindin B18 Peptide upon Binding to Lipid Membranes. A Solid-State NMR Study†

Biochemistry ◽  
2003 ◽  
Vol 42 (27) ◽  
pp. 8377-8386 ◽  
Author(s):  
Patrick Barré ◽  
Olaf Zschörnig ◽  
Klaus Arnold ◽  
Daniel Huster
Keyword(s):  
Solid State ◽  
Lipid Membranes ◽  
Solid State Nmr ◽  
Nmr Study

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.

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