Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property

Solid-state NMR has been used to study the influence of lipid bilayer hydrophobic thickness on the tilt of a peptide (M2-TMP) representing the transmembrane portion of the M2 protein from influenza A. Using anisotropic 15N chemical shifts as orientational constraints, single-site isotopically labele...

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Bibliographic Details
Published in:Journal of molecular biology 2000-01, Vol.295 (1), p.117-125
Main Authors: Kovacs, F.A., Denny, Jeffrey K., Song, Z., Quine, J.R., Cross, T.A.
Format: Article
Language:English
Subjects:
15N chemical shift
AM2 protein
Anisotropy
Circular Dichroism
Dimyristoylphosphatidylcholine - chemistry
Dimyristoylphosphatidylcholine - metabolism
Influenza A virus
Influenza A virus - chemistry
ion channel
Ion Channels - chemistry
Ion Channels - metabolism
Lipid Bilayers - chemistry
Lipid Bilayers - metabolism
Magnetic Resonance Spectroscopy
membrane protein
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Molecular Weight
orientational constraints
Phosphatidylcholines - chemistry
Phosphatidylcholines - metabolism
Protein Structure, Secondary
solid state NMR
Viral Matrix Proteins - chemistry
Viral Matrix Proteins - metabolism
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Summary:Solid-state NMR has been used to study the influence of lipid bilayer hydrophobic thickness on the tilt of a peptide (M2-TMP) representing the transmembrane portion of the M2 protein from influenza A. Using anisotropic 15N chemical shifts as orientational constraints, single-site isotopically labeled M2-TMPs were studied in hydrated dioleoylphosphatidylcholine (DOPC) and dimyristoylphosphatidylcholine (DMPC) lipid bilayers oriented between thin glass plates. These chemical shifts provide orientational information for the molecular frame with respect to the magnetic field in the laboratory frame. When modeled as a uniform ideal α-helix, M2-TMP has a tilt of 37(±3)° in DMPC and 33(±3)° in DOPC with respect to the bilayer normal in these lipid environments. The difference in helix tilt between the two environments appears to be small. This lack of a substantial change in tilt further suggests that significant interactions occur between the helices, as in an oligomeric state, to prevent a change in tilt in thicker lipid bilayers.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1999.3322