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Updated: Jul 19, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
Published on: August 15, 2014
CEESY: characterizing the conformation of unobservable protein states
Hugo van Ingen1, Geerten W Vuister, Sybren Wijmenga
1Department of Physical Chemistry, Radboud University Nijmegen, Toernooiveld 1, 6525 ED, Nijmegen, The Netherlands.
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.
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