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Journal Article

Evaluation of a shuttle DNP spectrometer by calculating the coupling and global enhancement factors of l-tryptophan.

MPS-Authors
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Lottmann,  P.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Bennati,  M.
Research Group of Electron Paramagnetic Resonance, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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http://www.springerlink.com/content/484m8h205q535w4l/fulltext.pdf
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Citation

Lottmann, P., Marquardsen, T., Krahn, A., Tavernier, A., Höfer, P., Bennati, M., et al. (2012). Evaluation of a shuttle DNP spectrometer by calculating the coupling and global enhancement factors of l-tryptophan. Applied Magnetic Resonance, 43(1-2), 207-221. doi:10.1007/s00723-012-0345-6.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-A5DB-0
Abstract
A liquid state shuttle dynamic nuclear polarization (DNP) spectrometer is presented, featuring several technical modifications that increase stability and improve reproducibility. For the protons of l-tryptophan, the signal enhancement and the DNP spin properties, such as relaxation, were measured and compared with each other. The calculated coupling factors suggest that the proton accessibility for the polarizer molecule has an important influence on the DNP enhancement. In general, short proton spin longitudinal relaxation times without radical reduce the detectable enhancement by decreasing the leakage factor and increasing the relaxation losses during the course of the sample transfer. The usage of a global enhancement factor gives a more complete overview of the capabilities for the described experimental setup. Global enhancements of up to −4.2 for l-tryptophan protons are found compared to pure Boltzmann enhancements of up to −2.4.