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Solid-state NMR provides unique possibilities to study insoluble or noncrystalline molecules at the atomic level. High-resolution conditions can be established by employing magic-angle spinning at ultrahigh magnetic fields. We discuss NMR methods that make use of these experimental improvements and allow for the study of multiply or uniformly [(13)C,(15)N]-labeled polypeptides and proteins. Recent biophysical applications are reviewed.
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Luca et al. (2003) studied this question.
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