Publication | Closed Access
Dynamic Nuclear Polarization of Deuterated Proteins
176
Citations
27
References
2010
Year
Magnetic Resonance SpectroscopyBiochemistryProtein AssemblyProtein FoldingGood FellowNatural SciencesResonanceMagnetic ResonanceMolecular BiologyNuclear Quadrupole ResonanceDynamic Nuclear PolarizationNuclear OrganizationNmr ExperimentsProtein NmrSolution Nmr SpectroscopyMedicineBiophysicsStructural Biology
For D's a jolly good fellow: Deuteration of proteins significantly increases the signal enhancements observed in dynamic nuclear polarization (DNP) magic-angle spinning (MAS) NMR experiments. In 13C CP-MAS spectra an enhancement of 120 is observed for perdeuterated SH3 with an exchangeable proton ratio of 50 %, whereas the enhancement is only 31 for the fully protonated SH3. The direct 13C excitation of the perdeuterated sample increases the enhancement to 148.
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