Governing function, half life and subcellular localization, the 3D structure and dynamics of proteins are in nature constantly changing in a tightly regulated manner to fulfill the physiological and adaptive requirements of the cells. To find evidence for this hypothesis, we applied in-cell NMR to three folded model proteins and propose that the splitting of cross peaks constitutes an atomic fingerprint of distinct structural states that arise from multiple target binding co-existing inside...
[ASAP] In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells
In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells
Rupam Ghosh, Yiling Xiao, Jaka Kragelj, and Kendra K. Frederick
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c06680/20211101/images/medium/ja1c06680_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.1c06680
http://feeds.feedburner.com/~r/acs/jacsat/~4/Px8tejOwLAA
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[NMR paper] In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells
In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells
NMR has the resolution and specificity to determine atomic-level protein structures of isotopically labeled proteins in complex environments, and with the sensitivity gains conferred by dynamic nuclear polarization (DNP), NMR has the sensitivity to detect proteins at their endogenous concentrations. However, DNP sensitivity enhancements are critically dependent on experimental conditions and sample composition. While some of these conditions are theoretically compatible with cellular viability,...
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[NMR paper] Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with their function. The semi-atomic resolution dynamics information revealed by NMR is able to discriminate function-related dynamics from random fluctuations. This review will discuss several studies in which quantitative dynamics information by solution......
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08-27-2021 03:49 PM
[NMR paper] In-Cell NMR of Intrinsically Disordered Proteins in Mammalian Cells.
In-Cell NMR of Intrinsically Disordered Proteins in Mammalian Cells.
Related Articles In-Cell NMR of Intrinsically Disordered Proteins in Mammalian Cells.
Methods Mol Biol. 2020;2141:873-893
Authors: Gerez JA, Prymaczok NC, Riek R
Abstract
In-cell NMR enables structural insights at atomic resolution of proteins in their natural environment. To date, very few methods have been developed to study proteins by in-cell NMR in mammalian systems. Here we describe a detailed protocol to conduct in-cell NMR on the intrinsically...
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07-23-2020 11:23 PM
[NMR paper] Recording In-Cell NMR-Spectra in Living Mammalian Cells.
Recording In-Cell NMR-Spectra in Living Mammalian Cells.
Related Articles Recording In-Cell NMR-Spectra in Living Mammalian Cells.
Methods Mol Biol. 2020;2141:857-871
Authors: Mate?ko-Burmann I, Burmann BM
Abstract
At the foundation of many cellular processes as well as a large number of diseases is the (mis)folding of important intrinsically disordered proteins (IDPs). Despite tremendous scientific efforts, the factors driving their structural changes within the cellular context remain poorly understood. In-cell NMR...
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[NMR paper] Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells.
Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells.
Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells.
Nat Protoc. 2016 Jun;11(6):1101-1111
Authors: Barbieri L, Luchinat E, Banci L
Abstract