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- W2019264211 abstract "While an increasing number of structural biology studies successfully demonstrate the power of high-resolution structures and dynamics of membrane proteins in fully understanding their function, there is considerable interest in developing NMR approaches to obtain such information in a cellular setting. As long as the proteins inside the living cell tumble rapidly in the NMR timescale, recently developed in-cell solution NMR approaches can provide 3D structural information. However, there are numerous challenges to study membrane proteins inside a cell. Research in our laboratory is focused on developing a combination of solid-state NMR and biological approaches to overcome these challenges in order to obtain high-resolution structural insights into electron transfer processes mediated by membrane-bound proteins like mammalian cytochrome-b5, cytochrome-P450 and cytochrome-P450-reductase. In this study, we demonstrate the feasibility of using dynamic nuclear polarization (DNP) magic angle spinning (MAS) NMR spectroscopy for in-cell studies on a membrane-anchored protein. Our experimental results obtained from ¹³C-labeled membrane-anchored cytochrome-b5 in native Escherichia coli cells show a ~16-fold DNP signal enhancement. Further, results obtained from a 2D ¹³C/¹³C chemical shift correlation MAS experiment demonstrate the feasibility of suppressing the background signals from other cellular contents for high-resolution structural studies on membrane proteins. We believe that this study would pave new avenues for high-resolution structural studies on a variety of membrane-associated proteins and their complexes in the cellular context to fully understand their functional roles in physiological processes." @default.
- W2019264211 created "2016-06-24" @default.
- W2019264211 creator A5006414766 @default.
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- W2019264211 creator A5088159992 @default.
- W2019264211 date "2015-01-01" @default.
- W2019264211 modified "2023-10-18" @default.
- W2019264211 title "Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization" @default.
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- W2019264211 doi "https://doi.org/10.1016/j.bbamem.2014.07.008" @default.
- W2019264211 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4258513" @default.
- W2019264211 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25017802" @default.
- W2019264211 hasPublicationYear "2015" @default.
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