Abstract
The transverse relaxation rates R 2 = 1/T 2 of protons can be determined by spin-echo sequences with multiple refocusing pulses using moderate radio-frequency field strengths and properly chosen inter-pulse delays so as to suppress echo modulations due to homonuclear scalar couplings. Combination with 2D heteronuclear correlation spectroscopy (HSQC) allows one to measure R 2 of arbitrary protons attached to nitrogen-15 or carbon-13 nuclei. Decays of six amide protons in the protein Ubiquitin that is nitrogen-15 enriched (but not deuterated) were measured at different temperatures.
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Acknowledgments
We thank Martial Rey for technical support and are indebted to the Swiss National Science Foundation, the Commission for Technology and Innovation, the Ecole Polytechnique Fédérale de Lausanne and the CNRS for funding.
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Segawa, T.F., Baishya, B. & Bodenhausen, G. Transverse Relaxation of Scalar Coupled Protons in Magnetic Resonance of Non-Deuterated Proteins. Appl Magn Reson 42, 353–361 (2012). https://doi.org/10.1007/s00723-011-0298-1
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DOI: https://doi.org/10.1007/s00723-011-0298-1