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An amphipathic alpha-helix controls multiple roles of brome mosaic virus protein 1a in RNA replication complex assembly and function.

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Table 2 shows that 65% of the observed NMR signals were assigned to specific atoms in the peptide
Fig. 6 shows that deleting helix A (1a D 35H, 1a D 18H) abrogated 1a’s ability to induce either type of ER membrane rearrangement.
Table 2. Titration results for BMV-1a helix A bound to SDS micelles with 16-DSA.
Figure 7. Class II mutations in 1a helix A induce hyper-abundant membrane invaginations
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