Comparison of "polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment

Vitaly V. Vostrikov; Christopher V. Grant; Anna E. Daily; Stanley J. Opella; Roger E. Koeppe

doi:10.1021/ja803734k

Comparison of "polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment

Vitaly V. Vostrikov, Christopher V. Grant, Anna E. Daily, Stanley J. Opella, Roger E. Koeppe

Chemical and Structural Biology (TMED)

Research output: Contribution to journal › Article › peer-review

52 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	12584-12585
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	130
Issue number	38
DOIs	https://doi.org/10.1021/ja803734k
State	Published - Sep 24 2008

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10.1021/ja803734k

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Comparison of "polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment. / Vostrikov, Vitaly V.; Grant, Christopher V.; Daily, Anna E. et al.
In: Journal of the American Chemical Society, Vol. 130, No. 38, 24.09.2008, p. 12584-12585.

Research output: Contribution to journal › Article › peer-review

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AU - Grant, Christopher V.

AU - Daily, Anna E.

AU - Opella, Stanley J.

AU - Koeppe, Roger E.

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N2 - 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.

AB - 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.

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Comparison of "polarization inversion with spin exchange at magic angle" and "geometric analysis of labeled alanines" methods for transmembrane helix alignment

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