Publication date: Available online 28 September 2014 Source:Journal of Magnetic Resonance
Author(s): Hassane. El Mkami , Richard Ward , Andrew Bowman , Tom Owen-Hughes , David G. Norman
Pulsed electron-electron double resonance (PELDOR) coupled with site-directed spin labeling is a powerful technique for the elucidation of protein or nucleic acid, macromolecular structure and interactions. The intrinsic high sensitivity of electron paramagnetic resonance enables measurement on small quantities of bio-macromolecules, however short relaxation times impose a limit on the sensitivity and size of distances that can be measured using this technique. The persistence of the electron spin-echo, in the PELDOR experiment, is one of the most crucial limitations to distance measurement. At a temperature of around 50 K one of the predominant factors affecting persistence of an echo, and as such, the sensitivity and measurable distance between spin labels, is the electron spin echo dephasing time (Tm). It has become normal practice to use deuterated solvents to extend Tm and recently it has been demonstrated that deuteration of the underlying protein significantly extends Tm. Here we examine the spatial effect of segmental deuteration of the underlying protein, and also explore the concentration and temperature dependence of highly deuterated systems. Graphical abstract
Spin dynamic simulations of solid effect DNP: the role of the relaxation superoperator
From The DNP-NMR Blog:
Spin dynamic simulations of solid effect DNP: the role of the relaxation superoperator
Karabanov, A., G. Kwiatkowski, and W. Köckenberger, Spin dynamic simulations of solid effect DNP: the role of the relaxation superoperator. Mol. Phys., 2014: p. 1-17.
http://dx.doi.org/10.1080/00268976.2014.884287
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From the The DNP-NMR Blog:
Effect of glassy modes on electron spin–lattice relaxation in solid ethanol
Merunka, D., et al., Effect of glassy modes on electron spin–lattice relaxation in solid ethanol. J. Magn. Reson., 2013. 228(0): p. 50-58.
http://www.ncbi.nlm.nih.gov/pubmed/23357426
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[Question from NMRWiki Q&A forum] Impact of deuteration on relaxation rates PROTEIN NMR
Impact of deuteration on relaxation rates PROTEIN NMR
DEAR NMR WIKIERS
IS THEIR ANY NMR EXPERMENT TO KNOW THE IMPACT OF DEUTERATION ON RELAXATION REATES OF C13,N15,H ALFA , H BETA OF DEURATED PROTEIN (RANDOMLY DEUTERTED) Regards
SRI
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The Spatial Effect of Protein Deuteration on Nitroxide Spin-label Relaxation: Implications for EPR Distance Measurement
Linear Mode
