George H. Jones coauthored structural and biochemical work on polynucleotide phosphorylase. The initial-only 2000 byline G. H. Jones is supplemented by the full byline in the collaborators' 2002 account and in a 2003 paper on enzyme purification.[ref]
Running rings around RNA: a superfamily of phosphate-dependent RNases by Martyn F. Symmons and others. Full byline
[ref]The 2003 work separated purified enzyme activity from possible contaminating nuclease activity by testing the dependence of degradation on phosphate. That distinction matters because polynucleotide phosphorylase uses phosphorolysis, whereas an unrelated hydrolytic nuclease could also make intact RNA disappear.[ref]
For an original control calculation, suppose intact-RNA signal falls by units with phosphate and by without it. Subtraction gives an increment of units associated with the changed condition. Interpreting all units as phosphate-dependent activity would ignore the background. Even the subtraction requires comparable samples, linear response and unchanged background behavior; it is not automatically a molecular rate measurement.
The shared 2000 X-ray crystallography paper supplied another kind of evidence: the architecture of a three-subunit protein complex. A structure can suggest where substrate recognition occurs, while biochemical controls test what chemical reaction the preparation actually performs.[ref]
A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation by M. F. Symmons and others. Abstract: trimeric architecture and catalytic-site interpretation
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