Detalle de: Transient structural ordering of the RNA-binding domain of carnation mottle virus p7 movement protein modulates nucleic acid binding

Plant viral movement proteins bind to RNA and participate in the intra‐ and intercellular movement of the RNAs from plant viruses. However, the role and magnitude of the conformational changes associated with the formation of RNA–protein complexes are not yet defined. Here we describe studies on the relevance of a preexisting nascent α‐helix at the C terminus of the RNA‐binding domain of p7, a movement protein from carnation mottle virus, to RNA binding. Synthetic peptide analogues and single amino acid mutation at the RNA‐binding domain of recombinant p7 protein were used to correlate the transient structural order in aqueous solution with RNA‐binding potential.