= James M. Murphy
{c}
<James M. Murphy> is a researcher in <protein> signaling and the functions of <pseudokinases>, kinase-like <protein domains> with altered residues normally associated with <catalysis>. In a 2014 collaborative study, <James M. Murphy> and colleagues developed a <thermal shift assay> to classify 31 <pseudokinase> <protein domains> according to their binding of <nucleotides> and metal ions.<A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties by James M. Murphy and others>[Abstract and classification results; Biochemical Journal 457, 323–334, 2014]{ref}
The key distinction is between binding and chemical activity. A <protein> may bind <ATP> without efficiently transferring its phosphate group. The <thermal shift assay> measures changes in thermal stability associated with binding, while an ordinary kinase activity assay can register activity from a small contaminating <protein kinase>. The study found four binding classes, including <pseudokinases> with no detectable binding and others whose binding depended on metal ions. This showed why the label <pseudokinase> cannot substitute for testing an individual <protein>.<A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties by James M. Murphy and others>[Abstract: four nucleotide/cation-binding classes and contamination caveat; Experimental: thermal-shift assays]{ref}
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