Journal
JOURNAL OF MAGNETIC RESONANCE
Volume 144, Issue 1, Pages 162-167Publisher
ACADEMIC PRESS INC
DOI: 10.1006/jmre.2000.2037
Keywords
PISEMA; N-15 solid-state NMR; orientational constraints; membrane proteins; oriented samples
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Resonance patterns have been observed in 2D solid-state NMR spectra of the transmembrane segment of M2 protein from Influenza A virus in oriented samples reflecting the helical wheel of this cu-helix, The center of this pattern uniquely defines the helical tilt with respect to the bilayer normal without a need for resonance assignments. The distribution of resonances from amino acid-specific labels around the PISA wheel defines the rotational orientation of the helix and yields preliminary site-specific assignments. With assignments high-resolution structural detail, such as differences in tilt and rotational orientation along the helical axis leading to an assessment of helical coiling, can be obtained. (C) 2000 Academic Press.
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