Orientational Distribution of α-Helices in the Colicin B and E1 Channel Domains:  A One and Two Dimensional 15N Solid-State NMR Investigation in Uniaxially Aligned Phospholipid Bilayers

Thermolytic fragments of the channel-forming bacterial toxins colicin B and colicin E1 were uniformly labeled with the 15N isotope and reconstituted into uniaxially oriented membranes. These well-aligned samples were investigated by proton-decoupled 15N solid-state NMR spectroscopy at 40.5 and 71.0...

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Veröffentlicht in:	Biochemistry (Easton) 1998-01, Vol.37 (1), p.16-22
Hauptverfasser:	Lambotte, Stephan, Jasperse, Pieter, Bechinger, Burkhard
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Colicins - chemistry Ion Channels - chemistry Lipid Bilayers - chemistry Magnetic Resonance Spectroscopy Membrane Proteins - chemistry Molecular Sequence Data Nitrogen Isotopes Phospholipids - chemistry Protein Structure, Secondary Protein Structure, Tertiary Thermodynamics
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