Comparison of “Polarization Inversion with Spin Exchange at Magic Angle” and “Geometric Analysis of Labeled Alanines” Methods for Transmembrane Helix Alignment

Using the model α-helical peptide acetyl−GGALW5LALALALALALALW19LAGA−ethanolamide (“GWALP23”), we have compared the polarization inversion with spin exchange at magic angle method and geometric analysis of labeled alanines method for estimating the transmembrane helix orientation. For GWALP23 in bila...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2008-09, Vol.130 (38), p.12584-12585
Main Authors: Vostrikov, Vitaly V, Grant, Christopher V, Daily, Anna E, Opella, Stanley J, Koeppe, Roger E
Format: Article
Language:English
Subjects:
Alanine - analogs & derivatives
Alanine - chemistry
Amides - chemistry
Ethanol - analogs & derivatives
Lipid Bilayers - chemistry
Nuclear Magnetic Resonance, Biomolecular - methods
Peptides - chemistry
Phosphatidylcholines - chemistry
Protein Structure, Secondary
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Summary:Using the model α-helical peptide acetyl−GGALW5LALALALALALALW19LAGA−ethanolamide (“GWALP23”), we have compared the polarization inversion with spin exchange at magic angle method and geometric analysis of labeled alanines method for estimating the transmembrane helix orientation. For GWALP23 in bilayers of a short lipid, dilauroylphosphatidylcholine, we find general agreement between the two methods, with a static helix tilt of about 11°−13° with respect to the bilayer normal.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja803734k