scholarly journals Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers

1998 ◽  
Vol 7 (2) ◽  
pp. 342-348 ◽  
Author(s):  
Yongae Kim ◽  
Kathleen Valentine ◽  
Stanley J. Opella ◽  
Sharon L. Schendel ◽  
William A. Cramer
Keyword(s):  
Solid State ◽  
Lipid Bilayers ◽  
Solid State Nmr ◽  
Nmr Studies ◽  
Closed State ◽  
Colicin E1 ◽  
Membrane Bound

Solid state NMR studies of membrances and membrane-bound systems

2000 ◽  
Vol 18 (4-5) ◽  
pp. 557
Author(s):  
David P. Weliky ◽  
Jun Yang ◽  
Charles Gabrys ◽  
Rong Yang ◽  
Christian Canlas ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Nmr Studies ◽  
Membrane Bound

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.

scholarly journals An Innovative Procedure Using a Sublimable Solid to Align Lipid Bilayers for Solid-State NMR Studies

2002 ◽  
Vol 82 (5) ◽  
pp. 2499-2503 ◽  
Author(s):  
Kevin J. Hallock ◽  
Katherine Henzler Wildman ◽  
Dong-Kuk Lee ◽  
Ayyalusamy Ramamoorthy
Keyword(s):  
Solid State ◽  
Lipid Bilayers ◽  
Solid State Nmr ◽  
Nmr Studies

scholarly journals Solid-State NMR Studies on the Membrane Bound Acylated Peptide Hormone Ghrelin

2012 ◽  
Vol 102 (3) ◽  
pp. 264a
Author(s):  
Gerrit Vortmeier ◽  
Constance Chollet ◽  
Holger A. Scheidt ◽  
Lars Thomas ◽  
Annette G. Beck-Sickinger ◽  
...  
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Peptide Hormone ◽  
Nmr Studies ◽  
Membrane Bound ◽  
Acylated Peptide

Solid-State NMR Studies of Full-Length BamA in Lipid Bilayers Suggest Limited Overall POTRA Mobility

2014 ◽  
Vol 426 (9) ◽  
pp. 2009-2021 ◽  
Author(s):  
Tessa Sinnige ◽  
Markus Weingarth ◽  
Marie Renault ◽  
Lindsay Baker ◽  
Jan Tommassen ◽  
...  
Keyword(s):  
Solid State ◽  
Lipid Bilayers ◽  
Solid State Nmr ◽  
Full Length ◽  
Nmr Studies
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