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Keywords:

  • backbone thioester exchange;
  • coiled coil;
  • fluorine;
  • NMR spectroscopy;
  • protein folding
Thumbnail image of graphical abstract

19F NMR to monitor BTE: A new strategy for assessing polypeptide tertiary structural stability by using thiol–thioester exchange is described. The backbone thioester exchange (BTE) method has previously been used to evaluate fold stability with HPLC measurements. Here we show that BTE can be followed by 19F NMR, which offers technical advantages. This technique was used for rapid identification of the most stable antiparallel coiled coil in a small library of new sequences.