Please use this identifier to cite or link to this item:
Title: CEESY: characterizing the conformation of unobservable protein states.
Authors: van Ingen H
Vuister, GW
Wijmenga, S
Tessari, M
First Published: 29-Mar-2006
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.
DOI Link: 10.1021/ja0568749
ISSN: 0002-7863
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

Files in This Item:
There are no files associated with this item.

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.