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Keywords:

  • excited states;
  • NMR spectroscopy;
  • protein dynamics;
  • protein folding;
  • structure elucidation
Thumbnail image of graphical abstract

Seeing the invisible: A 13CO NMR chemical exchange saturation transfer (CEST) experiment for the study of “invisible” excited protein states with lifetimes on the order of 5–50 ms has been developed. The 13CO chemical shifts together with those obtained from fits of 15N CEST profiles establish that the A39G FF domain folds via a similar compact intermediate (I) as the wild-type protein (F and U=native and unfolded states).