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|Title:||CEESY: characterizing the conformation of unobservable protein states.|
|Authors:||van Ingen H|
|Citation:||J AM CHEM SOC, 2006, 128 (12), pp. 3856-3857|
|Abstract:||Protein conformations that are only marginally populated often play important roles as intermediate states in many processes such as ligand binding, enzyme catalysis, allostery, and protein folding. An NMR method is presented that can give valuable information about the structure of these "excited states" by measuring the relative position of exchanging excited- and ground-state resonances using a single 2D spectrum. This new approach can be applied to any nucleus, which will facilitate a complete structural characterization of these states.|
|Appears in Collections:||Published Articles, Dept. of Biochemistry|
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