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REDOR NMR on a Hydrophobic Peptide in Oriented Membranes

✍ Scribed by David A Middleton; Zareen Ahmed; Clemens Glaubitz; Anthony Watts

Publisher: Elsevier Science
Year: 2000
Tongue: English
Weight: 114 KB
Volume: 147
Category: Article
ISSN: 1090-7807
DOI: 10.1006/jmre.2000.2187

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✦ Synopsis

A method is presented for the calculation of REDOR dephasing for specifically labeled membrane-spanning peptides in uniformly aligned lipid bilayers under magic angle oriented sample spinning (MAOSS) conditions. Numerical simulations are performed for dephasing of 13 C signal by 15 N when the labels are placed in an ␣-helical peptide at the carbonyl of residue (i) and amide nitrogen of residue (i ؉ 2) to show the dependency of REDOR echo intensity on the peptide tilt angle relative to the membrane normal. The approach was applied to the labeled transmembrane domain of phospholamban ([ 15 N-Leu 37 , 13 C-Leu 39 ]PLBTM) incorporated into dimyristoylphosphatidylcholine bilayers. The dephasing observed for a random membrane dispersion showed that the peptide was ␣-helical in the region including the two labels, and dephasing in oriented membranes showed that the peptide helix was tilted by 25°؎ 7°relative to the bilayer normal. These results agree with those obtained by other spectroscopic methods.

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