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- W2091657997 abstract "Inherent low sensitivity of NMR spectroscopy has been a major disadvantage, especially to study biomolecules like membrane proteins. Recent studies have successfully demonstrated the advantages of performing solid-state NMR experiments at very low and ultralow temperatures to enhance the sensitivity. However, the long spin–lattice relaxation time, T1, at very low temperatures is a major limitation. To overcome this difficulty, we demonstrate the use of a copper-chelated lipid for magic angle spinning solid-state NMR measurements on cytochrome-b5 reconstituted in multilamellar vesicles. Our results on multilamellar vesicles containing as small as 0.5 mol% of a copper-chelated lipid can significantly shorten T1 of protons, which can be used to considerably reduce the data collection time or to enhance the signal-to-noise ratio. We also monitored the effect of slow cooling on the resolution and sensitivity of 13C and 15N signals from the protein and 13C signals from lipids." @default.
- W2091657997 created "2016-06-24" @default.
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- W2091657997 date "2013-12-01" @default.
- W2091657997 modified "2023-10-18" @default.
- W2091657997 title "Shortening spin–lattice relaxation using a copper-chelated lipid at low-temperatures – A magic angle spinning solid-state NMR study on a membrane-bound protein" @default.
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- W2091657997 doi "https://doi.org/10.1016/j.jmr.2013.10.017" @default.
- W2091657997 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3868731" @default.
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