Duke biochemist linkurl:Homme Hellinga;http://www.biochem.duke.edu/faculty/homme-hellinga is facing another potential blow to his troubled career in protein and enzyme design.Hellinga has been linkurl:under investigation;http://www.the-scientist.com/blog/display/54889/ for possible research misconduct, following the linkurl:retraction;http://www.the-scientist.com/blog/display/54502/ of a Science paper on computational design of enzymes in February 2008. This week in the Proceedings of the National Academy of Sciences, Hellinga's former postdoc Birte Höcker and colleagues at the Max Planck Institute for Developmental Biology in Germany linkurl:dispute the conclusions;http://www.pnas.org/cgi/doi/10.1073/pnas.0907950106 of his studies on ligand-binding proteins, which appeared in linkurl:Nature in 2003;http://www.ncbi.nlm.nih.gov/pubmed/12736688 and linkurl:PNAS in 2004.;http://www.ncbi.nlm.nih.gov/pubmed/15148405 The interactions between ligands and their receptor are central to many biological processes and can potentially be tweaked to design novel biosensors and enzymes.The original papers from Hellinga's group purported to show that his team modified several proteins from E. coli in order to accept, for instance, the explosive TNT, instead of the sugars to which they normally cinch themselves...
The ScientistThe ScientistThe ScientistNatureJournal of Molecular BiologyThe ScientistScienceJournal of Molecular BiologyThe ScientistNaturePNASCorrection (October 14): The original version of the article incorrectly stated that the zinc biosensor did not bind to its ligand. In fact binding was observed, but it did not adopt the predicted shape change, suggesting it was not functioning properly.regrets the error.


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