Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.
 

Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.

Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy.

Angew Chem Int Ed Engl. 2013 Feb 28;

Authors: Vallurupalli P, Kay LE

Abstract
Seeing the invisible: A 13 CO 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 13 CO chemical shifts together with those obtained from fits of 15 N 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).


PMID: 23450751 [PubMed - as supplied by publisher]



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