Dispersion from C α or N H : 4D experiments for backbone resonance assignment of intrinsically disordered proteins
Dispersion from C α or N H : 4D experiments for backbone resonance assignment of intrinsically disordered proteins
Abstract
Resonance assignment of intrinsically disordered proteins is remarkably challenging due to scant chemical shift dispersion arising from conformational heterogeneity. The challenge is even greater if repeating segments are present in the amino acid sequence. To forward unambiguous resonance assignment of intrinsically disordered proteins, we present iHACANCO, HACACON and (HACA)CONCAHA, three Hα-detected 4D experiments with Cα...
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02-29-2020 09:52 PM
Triple resonance $$^{15}\hbox {N}$$ 15 N NMR relaxation experiments for studies of intrinsically disordered proteins
Triple resonance $$^{15}\hbox {N}$$ 15 N NMR relaxation experiments for studies of intrinsically disordered proteins
Abstract
Description of protein dynamics is known to be essential in understanding their function. Studies based on a well established \(^{15}\hbox {N}\) NMR relaxation methodology have been applied to a large number of systems....
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10-25-2017 10:14 PM
New 13C-detected experiments for the assignment of intrinsically disordered proteins
New 13C-detected experiments for the assignment of intrinsically disordered proteins
Abstract
NMR assignment of intrinsically disordered proteins (IDPs) by conventional HN-detected methods is hampered by the small dispersion of the amide protons chemical shifts and exchange broadening of amide proton signals. Therefore several alternative assignment strategies have been proposed in the last years. Attempting to seize that dispersion of 13Câ?² and 15N chemical shifts holds even in IDPs, we recently proposed two 13C-detected experiments to directly...
Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments - Frontiers
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