Imaging membrane protein helical wheels |
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Authors: | Wang J Denny J Tian C Kim S Mo Y Kovacs F Song Z Nishimura K Gan Z Fu R Quine J R Cross T A |
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Institution: | National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida 32310, USA. |
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Abstract: | 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 alpha-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. |
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