Unraveling the complexity of protein backbone dynamics with combined 13 C and 15 N solid-state NMR relaxation measurements
Typically, protein dynamics involve a complex hierarchy of motions occurring on different time scales between conformations separated by a range of different energy barriers. NMR relaxation can in principle provide a site-specific picture of both the time scales and amplitudes of these motions, but...
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Veröffentlicht in: | Physical chemistry chemical physics : PCCP 2015, Vol.17 (34), p.21997-22008 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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