Measurement of N15-T1 relaxation rates in a perdeuterated protein by magic angle spinning solid-state nuclear magnetic resonance spectroscopy
| العنوان: | Measurement of N15-T1 relaxation rates in a perdeuterated protein by magic angle spinning solid-state nuclear magnetic resonance spectroscopy |
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| المؤلفون: | Anne Diehl, Veniamin Chevelkov, Bernd Reif |
| المصدر: | The Journal of Chemical Physics. 128:052316 |
| بيانات النشر: | AIP Publishing, 2008. |
| سنة النشر: | 2008 |
| مصطلحات موضوعية: | Models, Molecular, Nitrogen Isotopes, Chemistry, Relaxation (NMR), Analytical chemistry, Spin–lattice relaxation, General Physics and Astronomy, Nuclear magnetic resonance spectroscopy, Deuterium, Spin–spin relaxation, Solid-state nuclear magnetic resonance, Magic angle spinning, Spin diffusion, Transverse relaxation-optimized spectroscopy, Protons, Physical and Theoretical Chemistry, Nuclear Magnetic Resonance, Biomolecular |
| الوصف: | In this paper, we present the measurement of (15)N-T(1) relaxation times in the solid state for a perdeuterated protein for which exchangeable protons are back substituted during recrystallization using a buffer which contains 10% H(2)O and 90% D(2)O. We find large variations of the (15)N relaxation time, even within the same beta sheet. By comparing (15)N-T(1) relaxation times measured for a protonated and a deuterated protein (using the above mentioned approach), we conclude that (1)H driven (15)N,(15)N spin diffusion has a significant impact on the absolute (15)N relaxation time in protonated proteins. This effect is important for a quantitative analysis of relaxation data in terms of molecular dynamics. |
| تدمد: | 1089-7690 0021-9606 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d0658e08639406f5af9370623728250Test https://doi.org/10.1063/1.2819311Test |
| رقم الانضمام: | edsair.doi.dedup.....9d0658e08639406f5af9370623728250 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10897690 00219606 |
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