High-field EPR spectroscopy applied to biological systems: characterization of molecular switches for electron and ion transfer

2005 ◽  
Vol 7 (1) ◽  
pp. 19-42 ◽  
Author(s):  
K. Möbius ◽  
A. Savitsky ◽  
A. Schnegg ◽  
M. Plato ◽  
M. Fuchs
Keyword(s):  
Epr Spectroscopy ◽  
High Field ◽  
Biological Systems ◽  
Molecular Switches ◽  
Ion Transfer

Solvent-free dynamic nuclear polarization enhancements in organically modified mesoporous silica

2021 ◽  
Author(s):  
Marcos de Oliveira Jr. ◽  
Kevin Herr ◽  
Martin Brodrecht ◽  
Nadia Berenice Haro-Mares ◽  
Till Wissel ◽  
...  
Keyword(s):  
Mesoporous Silica ◽  
Porous Materials ◽  
Structural Characterization ◽  
Dynamic Nuclear Polarization ◽  
High Field ◽  
Nuclear Polarization ◽  
Organically Modified ◽  
Field Dynamic ◽  
Free Dynamic

High-field Dynamic Nuclear Polarization is a powerful tool for the structural characterization of species on the surface of porous materials or nanoparticles. For these studies the main source of polarization...

scholarly journals How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?

2021 ◽  
Vol 75 (2-3) ◽  
pp. 119-131
Author(s):  
Albert A. Smith ◽  
Nicolas Bolik-Coulon ◽  
Matthias Ernst ◽  
Beat H. Meier ◽  
Fabien Ferrage
Keyword(s):  
Nuclear Magnetic Resonance ◽  
High Resolution ◽  
High Field ◽  
Rotational Diffusion ◽  
Relaxation Data ◽  
Internal Dynamics ◽  
Nmr Relaxometry ◽  
Analysis Of Dynamics

AbstractThe dynamics of molecules in solution is usually quantified by the determination of timescale-specific amplitudes of motions. High-resolution nuclear magnetic resonance (NMR) relaxometry experiments—where the sample is transferred to low fields for longitudinal (T1) relaxation, and back to high field for detection with residue-specific resolution—seeks to increase the ability to distinguish the contributions from motion on timescales slower than a few nanoseconds. However, tumbling of a molecule in solution masks some of these motions. Therefore, we investigate to what extent relaxometry improves timescale resolution, using the “detector” analysis of dynamics. Here, we demonstrate improvements in the characterization of internal dynamics of methyl-bearing side chains by carbon-13 relaxometry in the small protein ubiquitin. We show that relaxometry data leads to better information about nanosecond motions as compared to high-field relaxation data only. Our calculations show that gains from relaxometry are greater with increasing correlation time of rotational diffusion.

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