ABSTRACT
Proteins....................................................................................................... 227 12.5 ENMR of Proteins in Biological Buffer Solutions ................................... 230 12.6 Two-Dimensional ENMR Signal Separation of Coexisting Proteins in
Solution ...................................................................................................... 233 12.6.1 Measurement of Electrophoretic Mobility Distributions by
2D ENMR...................................................................................... 233 12.6.2 Two-Dimensional ENMR of Proteins and Protein Mixtures ....... 235 12.6.3 Enhanced 2D ENMR Resolution by Maximum Entropy Method.... 236
12.7 Three-Dimensional ENMR ........................................................................ 237 12.8 Ex-ENMR Characterization of Protein Reaction Interfaces ..................... 241 12.9 Microcoil ENMR Using a Single Horizontal Capillary............................ 243 12.10 Constant-Time Multidimensional ENMR for Horizontal Sample Tubes.... 245 12.11 Future Prospects ......................................................................................... 247 Acknowledgments.................................................................................................. 249 References.............................................................................................................. 249
Electrophoretic nuclear magnetic resonance (ENMR) has the potential of becoming an important proteomic technique. The method offers possible structural characterization of protein interactions in biological signaling processes. The proteomic analyses currently employed offer separation-based methods using two-dimensional gel electrophoresis or mass spectrometry to identify proteins. In these proteomic analyses, information on protein structures is lost and therefore the methods cannot be used to characterize protein conformational changes in biochemical reactions.
