An RNA helicase is a protein activity that separates paired RNA strands or opens local RNA secondary structure. Strand separation concerns noncovalent pairing; it is different from cutting the phosphodiester bonds in the RNA backbone. The way a helicase couples nucleotide binding, energy use and structural change depends on the protein, so an unwinding observation does not alone specify its mechanism.[ref]
How RNase R Degrades Structured RNA: Role of the Helicase Activity and the S1 Domain by Sk Tofajjen Hossain and others. Abstract: intrinsic RNA helicase, ATP binding and nuclease activities distinguished
For an inventory example, consider a duplex formed by two 12-nucleotide RNA strands. Separation without cleavage leaves two 12-nucleotide strands and 24 nucleotides in total. Cleavage would instead change the lengths of covalent chains. A falling duplex signal could therefore reflect unwinding, degradation or both unless the measurement distinguishes these outcomes.
A 2016 study of RNase R made that separation experimentally: designed RNA substrates and an altered nuclease-deficient protein were used to examine strand separation independently of normal RNA degradation. ATP-binding assays and fluorescence measurements supplied different evidence about binding and conformational change.[ref]
How RNase R Degrades Structured RNA: Role of the Helicase Activity and the S1 Domain by Sk Tofajjen Hossain and others. Abstract; Figures1–2: designed duplexes, RNase R D272N and ATP-binding measurements
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