There?s linkurl:a pretty slick paper;http://www.nature.com/nmeth/journal/v3/n2/abs/nmeth851.html in the February __Nature Methods__. Alexander Shekhtman, of SUNY-Albany, describes a novel technique called STINT-NMR (for structural interactions using in-cell NMR), which maps a protein?s structural changes in response to protein-protein interactions in vivo. Shekhtman presented his work Tuesday (Jan. 31) at the Keystone Symposium on Structural Genomics, and I got the chance to talk to him about it during this evening?s poster sessions. As Shekhtman explains, most protein-protein mapping strategies (the yeast two-hybrid assay and affinity purification-mass spectrometry, for instance) reveal binary data: either an interaction occurs or it doesn?t. They say nothing about interaction surfaces, nor do they illuminate the broad structural changes that can result from protein docking events. In STINT-NMR Shekhtman sequentially overexpresses two (or more) proteins in bacteria, using different reagents to control the timing of induction. The first protein is grown in isotopically labeled media (that is, media containing...
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