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Probing Slow Chemical Exchange at Carbonyl Sites in Proteins by Chemical Exchange Saturation Transfer NMR Spectroscopy
Author(s) -
Vallurupalli Pramodh,
Kay Lewis E.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201209118
Subject(s) - saturation (graph theory) , chemical shift , nuclear magnetic resonance spectroscopy , excited state , spectroscopy , chemistry , computer science , chemical physics , physics , atomic physics , stereochemistry , mathematics , combinatorics , quantum mechanics
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).